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Novus Biologicals βiii spectrin

a, Schematic of βII and <t>βIII</t> spectrins expression in the somatodendritic compartment, axon initial segment (AIS) and distal unmyelinated axon. b, Comparison of βII and βIII spectrins sequences and binding domains. c, d, e, Representative confocal images for <t>βII-spectrin</t> (orange), βIII-spectrin (magenta), CAAX-GFP (grey) and Homer1C (cyan) in a filopodium (a), a mature spine (b) or a dendrite (c) at 21 DIV. Scale bars, 1 µm for filopodium and spine, 2 µm for dendrite. Note that the display contrast was purposely kept constant. f, g, Fluorescence intensity of βII-spectrin and βIII-spectrin in spine necks and dendrites at 10 DIV and 21 DIV normalized to the average intensity of filopodia at the same time-point. Each box shows the median ± percentile. n between 98 and 160 spines or 84 and 97 dendrites from 20 to 30 neurons examined over 3 independent experiments for each time point. Mann-Whitney test, *: p < 0.05, ***: p < 0.001, ****: p < 0.0001. h, i, Correlation scatter plots between βII-spectrin and βIII-spectrin normalized fluorescence intensities in spine neck or dendrite at 10 DIV and 21 DIV. n between 98 and 160 spines or 84 and 97 dendrites from 20 to 30 neurons examined over 3 independent experiments for each time point. r , Pearson’s r coefficient; P, P value.

βiii Spectrin, supplied by Novus Biologicals, used in various techniques. Bioz Stars score: 94/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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1) Product Images from "βII and βIII spectrin paralogues define robustness and specialization of the neuronal membrane periodic skeleton"

Article Title: βII and βIII spectrin paralogues define robustness and specialization of the neuronal membrane periodic skeleton

Journal: bioRxiv

doi: 10.64898/2026.03.23.713115

a, Schematic of βII and βIII spectrins expression in the somatodendritic compartment, axon initial segment (AIS) and distal unmyelinated axon. b, Comparison of βII and βIII spectrins sequences and binding domains. c, d, e, Representative confocal images for βII-spectrin (orange), βIII-spectrin (magenta), CAAX-GFP (grey) and Homer1C (cyan) in a filopodium (a), a mature spine (b) or a dendrite (c) at 21 DIV. Scale bars, 1 µm for filopodium and spine, 2 µm for dendrite. Note that the display contrast was purposely kept constant. f, g, Fluorescence intensity of βII-spectrin and βIII-spectrin in spine necks and dendrites at 10 DIV and 21 DIV normalized to the average intensity of filopodia at the same time-point. Each box shows the median ± percentile. n between 98 and 160 spines or 84 and 97 dendrites from 20 to 30 neurons examined over 3 independent experiments for each time point. Mann-Whitney test, *: p < 0.05, ***: p < 0.001, ****: p < 0.0001. h, i, Correlation scatter plots between βII-spectrin and βIII-spectrin normalized fluorescence intensities in spine neck or dendrite at 10 DIV and 21 DIV. n between 98 and 160 spines or 84 and 97 dendrites from 20 to 30 neurons examined over 3 independent experiments for each time point. r , Pearson’s r coefficient; P, P value.

Figure Legend Snippet: a, Schematic of βII and βIII spectrins expression in the somatodendritic compartment, axon initial segment (AIS) and distal unmyelinated axon. b, Comparison of βII and βIII spectrins sequences and binding domains. c, d, e, Representative confocal images for βII-spectrin (orange), βIII-spectrin (magenta), CAAX-GFP (grey) and Homer1C (cyan) in a filopodium (a), a mature spine (b) or a dendrite (c) at 21 DIV. Scale bars, 1 µm for filopodium and spine, 2 µm for dendrite. Note that the display contrast was purposely kept constant. f, g, Fluorescence intensity of βII-spectrin and βIII-spectrin in spine necks and dendrites at 10 DIV and 21 DIV normalized to the average intensity of filopodia at the same time-point. Each box shows the median ± percentile. n between 98 and 160 spines or 84 and 97 dendrites from 20 to 30 neurons examined over 3 independent experiments for each time point. Mann-Whitney test, *: p < 0.05, ***: p < 0.001, ****: p < 0.0001. h, i, Correlation scatter plots between βII-spectrin and βIII-spectrin normalized fluorescence intensities in spine neck or dendrite at 10 DIV and 21 DIV. n between 98 and 160 spines or 84 and 97 dendrites from 20 to 30 neurons examined over 3 independent experiments for each time point. r , Pearson’s r coefficient; P, P value.

Techniques Used: Expressing, Comparison, Binding Assay, Fluorescence, MANN-WHITNEY

a, b, c, Representative d STORM images of βII-spectrin and its 1D autocorrelation amplitude in axons (a), dendrites (b), and spine necks with PSD95 labelling observed in epifluorescence (c). The non-periodic control was obtained by measuring the 1D autocorrelation amplitude of a cytosolic mCherry labelling in axons, dendrites or spine necks. n between 45 and 80 regions of interest examined over at least 3 independent experiments. d, Spacing between βII-spectrin epitopes. e, f, Representative d STORM images of βIII-spectrin and its 1D autocorrelation amplitude in dendrites (e) and spine necks (f). n between 45 and 80 regions of interest examined over at least 3 independent experiments. g, Spacing between βIII-spectrin epitopes. h, i, Representative two-color STORM images of βII-spectrin and βIII-spectrin and autocorrelation (AC) or cross-correlation amplitudes in dendrites (h) and spine necks with Homer1C labelling (i). n = 76 regions of interest examined over 3 independent experiments. j, Spacing between β-spectrin epitopes after merging the two channels. Each box shows the median ± percentile. Scale bars, 1 µm. Mann-Whitney test, ns: non-significant, ****: p < 0.0001.

Figure Legend Snippet: a, b, c, Representative d STORM images of βII-spectrin and its 1D autocorrelation amplitude in axons (a), dendrites (b), and spine necks with PSD95 labelling observed in epifluorescence (c). The non-periodic control was obtained by measuring the 1D autocorrelation amplitude of a cytosolic mCherry labelling in axons, dendrites or spine necks. n between 45 and 80 regions of interest examined over at least 3 independent experiments. d, Spacing between βII-spectrin epitopes. e, f, Representative d STORM images of βIII-spectrin and its 1D autocorrelation amplitude in dendrites (e) and spine necks (f). n between 45 and 80 regions of interest examined over at least 3 independent experiments. g, Spacing between βIII-spectrin epitopes. h, i, Representative two-color STORM images of βII-spectrin and βIII-spectrin and autocorrelation (AC) or cross-correlation amplitudes in dendrites (h) and spine necks with Homer1C labelling (i). n = 76 regions of interest examined over 3 independent experiments. j, Spacing between β-spectrin epitopes after merging the two channels. Each box shows the median ± percentile. Scale bars, 1 µm. Mann-Whitney test, ns: non-significant, ****: p < 0.0001.

Techniques Used: Control, MANN-WHITNEY

a, Schematic of βII-, βIII- and ɑII-spectrin in the dendrite. Arrowheads correspond to the same area. b , Quantification of the distances between clusters of localizations on XZ projections. c-f , Two-color 3D MINFLUX of βII- and βIII-spectrins in dendrite (c and d) and dendritic spine neck (e and f). Scale bars, 500 nm in c and e, 100 nm in d and f. Arrowheads highlight clusters of localizations that appear in pairs, independently of the β-spectrin isoform, mostly visible in dendrites. (d) and (f) XZ projections of regions in (c) and (e) respectively, show discrete clusters regularly spaced independently of the β-spectrin paralogue, suggesting that βII- and βIII-spectrins are radially periodic.

Figure Legend Snippet: a, Schematic of βII-, βIII- and ɑII-spectrin in the dendrite. Arrowheads correspond to the same area. b , Quantification of the distances between clusters of localizations on XZ projections. c-f , Two-color 3D MINFLUX of βII- and βIII-spectrins in dendrite (c and d) and dendritic spine neck (e and f). Scale bars, 500 nm in c and e, 100 nm in d and f. Arrowheads highlight clusters of localizations that appear in pairs, independently of the β-spectrin isoform, mostly visible in dendrites. (d) and (f) XZ projections of regions in (c) and (e) respectively, show discrete clusters regularly spaced independently of the β-spectrin paralogue, suggesting that βII- and βIII-spectrins are radially periodic.

Techniques Used:

a, b, c, Representative d STORM images of βII-spectrin in a βIII-spectrin KO axon (a), dendrite (b) and spine (c), followed by βII-spectrin localization intensities, 1D autocorrelation amplitudes and spacing measured in the associated neurites. The non-periodic controls are the same as in . PSD95 was imaged using epifluorescence microscopy. n between 30 and 88 regions of interest per neurite examined over 5 independent experiments. d, e, Representative d STORM images of βIII-spectrin in a βII-spectrin KO dendrite (d) and spine (e), followed by βIII-spectrin localizations intensities, 1D autocorrelation amplitudes and spacing measured in the associated neurites. n between 30 and 88 regions of interest per neurite examined over at least 3 independent experiments. Each box represents the median with percentile. Scale bars, 1 µm. Mann-Whitney tests, ns: non-significant, *: p < 0.05, ****: p < 0.0001.

Figure Legend Snippet: a, b, c, Representative d STORM images of βII-spectrin in a βIII-spectrin KO axon (a), dendrite (b) and spine (c), followed by βII-spectrin localization intensities, 1D autocorrelation amplitudes and spacing measured in the associated neurites. The non-periodic controls are the same as in . PSD95 was imaged using epifluorescence microscopy. n between 30 and 88 regions of interest per neurite examined over 5 independent experiments. d, e, Representative d STORM images of βIII-spectrin in a βII-spectrin KO dendrite (d) and spine (e), followed by βIII-spectrin localizations intensities, 1D autocorrelation amplitudes and spacing measured in the associated neurites. n between 30 and 88 regions of interest per neurite examined over at least 3 independent experiments. Each box represents the median with percentile. Scale bars, 1 µm. Mann-Whitney tests, ns: non-significant, *: p < 0.05, ****: p < 0.0001.

Techniques Used: Epifluorescence Microscopy, MANN-WHITNEY

a, b, c, Representative d STORM images of ɑII-spectrin in control or KOs axons (a), dendrites (b) and spines (c), followed by ɑII-spectrin mean intensities, 1D autocorrelation amplitudes and spacing measured in the corresponding compartments. Only conditions where ɑII-spectrin mean intensity median value was above one-quarter of the controls ɑ2-spectrin values were analysed for autocorrelation and spacing. The non-periodic controls are the same as . PSD95 was imaged using epifluorescence microscopy. n between 14 and 53 regions of interest per neurite examined over 3 independent experiments. Each box represents the median with percentile. Scale bars, 1 µm. Mann-Whitney tests, ns: non-significant, *: p < 0.05, **: p < 0.01, ***: p < 0.001, ****: p < 0.0001.

Figure Legend Snippet: a, b, c, Representative d STORM images of ɑII-spectrin in control or KOs axons (a), dendrites (b) and spines (c), followed by ɑII-spectrin mean intensities, 1D autocorrelation amplitudes and spacing measured in the corresponding compartments. Only conditions where ɑII-spectrin mean intensity median value was above one-quarter of the controls ɑ2-spectrin values were analysed for autocorrelation and spacing. The non-periodic controls are the same as . PSD95 was imaged using epifluorescence microscopy. n between 14 and 53 regions of interest per neurite examined over 3 independent experiments. Each box represents the median with percentile. Scale bars, 1 µm. Mann-Whitney tests, ns: non-significant, *: p < 0.05, **: p < 0.01, ***: p < 0.001, ****: p < 0.0001.

Techniques Used: Control, Epifluorescence Microscopy, MANN-WHITNEY

$a, Scheme of βII- and βIII-spectrins highlighting the mutations disrupting interaction with phosphoinositides, ankyrins or actin. b, c, Representative spinning disk images of neurons re-expressing βII- (a) or βIII-spectrins (b) WT and mutant all tagged with eGFP, and expressing an intrabody labelling PSD95 . Scale bars in top images, 20 µm. Scale bars in bottom images, 1 µm. d, e, Ratios of the mean fluorescence intensity measured in axons, dendrites and spines in endogenous and re-expression conditions. n between 9 and 22 neurons obtained from 3 to 5 independent experiments for βII-spectrin, n between 7 and 16 neurons obtained from 3 to 4 independent experiments for βIII-spectrin. f, g, Mobile fractions of βII/III-spectrins measured 180 seconds after photobleaching. Each box represents the median with percentile. n between 12 and 24 regions of interest per neurite obtained from 3 to 5 independent experiments for βII-spectrin, n between 13 and 18 regions of interest per neurite obtained from 3 to 4 independent experiments for βIII-spectrin. Each box represents the median with percentile. Mann-Whitney tests, ns: non-significant, *: p < 0.05, **: p < 0.01, ***: p < 0.001, ****: p < 0.0001.$
Figure Legend Snippet: a, Scheme of βII- and βIII-spectrins highlighting the mutations disrupting interaction with phosphoinositides, ankyrins or actin. b, c, Representative spinning disk images of neurons re-expressing βII- (a) or βIII-spectrins (b) WT and mutant all tagged with eGFP, and expressing an intrabody labelling PSD95 . Scale bars in top images, 20 µm. Scale bars in bottom images, 1 µm. d, e, Ratios of the mean fluorescence intensity measured in axons, dendrites and spines in endogenous and re-expression conditions. n between 9 and 22 neurons obtained from 3 to 5 independent experiments for βII-spectrin, n between 7 and 16 neurons obtained from 3 to 4 independent experiments for βIII-spectrin. f, g, Mobile fractions of βII/III-spectrins measured 180 seconds after photobleaching. Each box represents the median with percentile. n between 12 and 24 regions of interest per neurite obtained from 3 to 5 independent experiments for βII-spectrin, n between 13 and 18 regions of interest per neurite obtained from 3 to 4 independent experiments for βIII-spectrin. Each box represents the median with percentile. Mann-Whitney tests, ns: non-significant, *: p < 0.05, **: p < 0.01, ***: p < 0.001, ****: p < 0.0001.

Techniques Used: Expressing, Mutagenesis, Fluorescence, MANN-WHITNEY

a, b Representative d STORM images of wild-type and mutant βII-spectrins (a) and wild-type and mutant βIII-spectrins (b) imaged in re-expression condition in the indicated neuronal compartments. The non-periodic controls are the same as in . PSD95 was imaged using epifluorescence microscopy. Scale bars, 1 µm. c, d βII-spectrin (a) and βIII-spectrins (b) 1D autocorrelation amplitudes measured in the indicated compartments. n between 31 and 162 regions of interest per compartment obtained from 3 to 5 independent experiments for βII-spectrin. n between 73 and 213 regions of interest per compartment obtained from 3 to 4 independent experiments βIII-spectrins. Each box represents the median with percentile. Mann-Whitney tests, ns: non-significant, *: p < 0.05, **: p < 0.01, ****: p < 0.0001. e, f, Spacing between βII-spectrin (e) or βIII-spectrin (f) epitopes obtained from the same datasets as in (c) and (d).

Figure Legend Snippet: a, b Representative d STORM images of wild-type and mutant βII-spectrins (a) and wild-type and mutant βIII-spectrins (b) imaged in re-expression condition in the indicated neuronal compartments. The non-periodic controls are the same as in . PSD95 was imaged using epifluorescence microscopy. Scale bars, 1 µm. c, d βII-spectrin (a) and βIII-spectrins (b) 1D autocorrelation amplitudes measured in the indicated compartments. n between 31 and 162 regions of interest per compartment obtained from 3 to 5 independent experiments for βII-spectrin. n between 73 and 213 regions of interest per compartment obtained from 3 to 4 independent experiments βIII-spectrins. Each box represents the median with percentile. Mann-Whitney tests, ns: non-significant, *: p < 0.05, **: p < 0.01, ****: p < 0.0001. e, f, Spacing between βII-spectrin (e) or βIII-spectrin (f) epitopes obtained from the same datasets as in (c) and (d).

Techniques Used: Mutagenesis, Expressing, Epifluorescence Microscopy, MANN-WHITNEY

a, Schematic of the periodic actin-spectrin cytoskeleton in axons (βII-spectrin mostly), dendrites and dendritic spines (random βII and βIII spectrins distribution with the presence of sparse βII/βIII heterotypic tetramers). Spectrin signals are excluded from post-synaptic densities. b, Schematic of βII- and βIII-spectrins sensitivity to their binding partners.

Figure Legend Snippet: a, Schematic of the periodic actin-spectrin cytoskeleton in axons (βII-spectrin mostly), dendrites and dendritic spines (random βII and βIII spectrins distribution with the presence of sparse βII/βIII heterotypic tetramers). Spectrin signals are excluded from post-synaptic densities. b, Schematic of βII- and βIII-spectrins sensitivity to their binding partners.

Techniques Used: Binding Assay

Image Search Results

Journal: bioRxiv

Article Title: βII and βIII spectrin paralogues define robustness and specialization of the neuronal membrane periodic skeleton

doi: 10.64898/2026.03.23.713115

Figure Lengend Snippet: a, Schematic of βII and βIII spectrins expression in the somatodendritic compartment, axon initial segment (AIS) and distal unmyelinated axon. b, Comparison of βII and βIII spectrins sequences and binding domains. c, d, e, Representative confocal images for βII-spectrin (orange), βIII-spectrin (magenta), CAAX-GFP (grey) and Homer1C (cyan) in a filopodium (a), a mature spine (b) or a dendrite (c) at 21 DIV. Scale bars, 1 µm for filopodium and spine, 2 µm for dendrite. Note that the display contrast was purposely kept constant. f, g, Fluorescence intensity of βII-spectrin and βIII-spectrin in spine necks and dendrites at 10 DIV and 21 DIV normalized to the average intensity of filopodia at the same time-point. Each box shows the median ± percentile. n between 98 and 160 spines or 84 and 97 dendrites from 20 to 30 neurons examined over 3 independent experiments for each time point. Mann-Whitney test, *: p < 0.05, ***: p < 0.001, ****: p < 0.0001. h, i, Correlation scatter plots between βII-spectrin and βIII-spectrin normalized fluorescence intensities in spine neck or dendrite at 10 DIV and 21 DIV. n between 98 and 160 spines or 84 and 97 dendrites from 20 to 30 neurons examined over 3 independent experiments for each time point. r , Pearson’s r coefficient; P, P value.

Article Snippet: The following primary antibodies were used: βII-spectrin (BD Biosciences, 612 563, mouse IgG1 monoclonal, 1/500), βIII-spectrin (Novus Biotechnologies, NB110 58346, rabbit polyclonal, 1/500 or Santa Cruz, sc515737, monoclonal, 1/100), αII-spectrin (Biolegend, 803206, mouse IgG2b monoclonal, 1/1000), α-Adducin (Abcam, 51130, rabbit IgG polyclonal, 1/200), GFP (Avès, GFP-1020, chicken monoclonal, 1/2000), DsRed (Takara, 632496, rabbit polyclonal, 1/2000), PSD-95 (ThermoFisher, MA1-046, mouse IgG1 monoclonal, 1/500), Homer 1C (Synaptic Systems, 160004, guinea pig polyclonal, 1/500).

Techniques: Expressing, Comparison, Binding Assay, Fluorescence, MANN-WHITNEY

Journal: bioRxiv

Article Title: βII and βIII spectrin paralogues define robustness and specialization of the neuronal membrane periodic skeleton

doi: 10.64898/2026.03.23.713115

Figure Lengend Snippet: a, b, c, Representative d STORM images of βII-spectrin and its 1D autocorrelation amplitude in axons (a), dendrites (b), and spine necks with PSD95 labelling observed in epifluorescence (c). The non-periodic control was obtained by measuring the 1D autocorrelation amplitude of a cytosolic mCherry labelling in axons, dendrites or spine necks. n between 45 and 80 regions of interest examined over at least 3 independent experiments. d, Spacing between βII-spectrin epitopes. e, f, Representative d STORM images of βIII-spectrin and its 1D autocorrelation amplitude in dendrites (e) and spine necks (f). n between 45 and 80 regions of interest examined over at least 3 independent experiments. g, Spacing between βIII-spectrin epitopes. h, i, Representative two-color STORM images of βII-spectrin and βIII-spectrin and autocorrelation (AC) or cross-correlation amplitudes in dendrites (h) and spine necks with Homer1C labelling (i). n = 76 regions of interest examined over 3 independent experiments. j, Spacing between β-spectrin epitopes after merging the two channels. Each box shows the median ± percentile. Scale bars, 1 µm. Mann-Whitney test, ns: non-significant, ****: p < 0.0001.

Techniques: Control, MANN-WHITNEY

Journal: bioRxiv

Article Title: βII and βIII spectrin paralogues define robustness and specialization of the neuronal membrane periodic skeleton

doi: 10.64898/2026.03.23.713115

Figure Lengend Snippet: a, Schematic of βII-, βIII- and ɑII-spectrin in the dendrite. Arrowheads correspond to the same area. b , Quantification of the distances between clusters of localizations on XZ projections. c-f , Two-color 3D MINFLUX of βII- and βIII-spectrins in dendrite (c and d) and dendritic spine neck (e and f). Scale bars, 500 nm in c and e, 100 nm in d and f. Arrowheads highlight clusters of localizations that appear in pairs, independently of the β-spectrin isoform, mostly visible in dendrites. (d) and (f) XZ projections of regions in (c) and (e) respectively, show discrete clusters regularly spaced independently of the β-spectrin paralogue, suggesting that βII- and βIII-spectrins are radially periodic.

Techniques:

Journal: bioRxiv

Article Title: βII and βIII spectrin paralogues define robustness and specialization of the neuronal membrane periodic skeleton

doi: 10.64898/2026.03.23.713115

Figure Lengend Snippet: a, b, c, Representative d STORM images of βII-spectrin in a βIII-spectrin KO axon (a), dendrite (b) and spine (c), followed by βII-spectrin localization intensities, 1D autocorrelation amplitudes and spacing measured in the associated neurites. The non-periodic controls are the same as in . PSD95 was imaged using epifluorescence microscopy. n between 30 and 88 regions of interest per neurite examined over 5 independent experiments. d, e, Representative d STORM images of βIII-spectrin in a βII-spectrin KO dendrite (d) and spine (e), followed by βIII-spectrin localizations intensities, 1D autocorrelation amplitudes and spacing measured in the associated neurites. n between 30 and 88 regions of interest per neurite examined over at least 3 independent experiments. Each box represents the median with percentile. Scale bars, 1 µm. Mann-Whitney tests, ns: non-significant, *: p < 0.05, ****: p < 0.0001.

Techniques: Epifluorescence Microscopy, MANN-WHITNEY

Journal: bioRxiv

Article Title: βII and βIII spectrin paralogues define robustness and specialization of the neuronal membrane periodic skeleton

doi: 10.64898/2026.03.23.713115

Figure Lengend Snippet: a, b, c, Representative d STORM images of ɑII-spectrin in control or KOs axons (a), dendrites (b) and spines (c), followed by ɑII-spectrin mean intensities, 1D autocorrelation amplitudes and spacing measured in the corresponding compartments. Only conditions where ɑII-spectrin mean intensity median value was above one-quarter of the controls ɑ2-spectrin values were analysed for autocorrelation and spacing. The non-periodic controls are the same as . PSD95 was imaged using epifluorescence microscopy. n between 14 and 53 regions of interest per neurite examined over 3 independent experiments. Each box represents the median with percentile. Scale bars, 1 µm. Mann-Whitney tests, ns: non-significant, *: p < 0.05, **: p < 0.01, ***: p < 0.001, ****: p < 0.0001.

Techniques: Control, Epifluorescence Microscopy, MANN-WHITNEY

Journal: bioRxiv

Article Title: βII and βIII spectrin paralogues define robustness and specialization of the neuronal membrane periodic skeleton

doi: 10.64898/2026.03.23.713115

Figure Lengend Snippet: a, Scheme of βII- and βIII-spectrins highlighting the mutations disrupting interaction with phosphoinositides, ankyrins or actin. b, c, Representative spinning disk images of neurons re-expressing βII- (a) or βIII-spectrins (b) WT and mutant all tagged with eGFP, and expressing an intrabody labelling PSD95 . Scale bars in top images, 20 µm. Scale bars in bottom images, 1 µm. d, e, Ratios of the mean fluorescence intensity measured in axons, dendrites and spines in endogenous and re-expression conditions. n between 9 and 22 neurons obtained from 3 to 5 independent experiments for βII-spectrin, n between 7 and 16 neurons obtained from 3 to 4 independent experiments for βIII-spectrin. f, g, Mobile fractions of βII/III-spectrins measured 180 seconds after photobleaching. Each box represents the median with percentile. n between 12 and 24 regions of interest per neurite obtained from 3 to 5 independent experiments for βII-spectrin, n between 13 and 18 regions of interest per neurite obtained from 3 to 4 independent experiments for βIII-spectrin. Each box represents the median with percentile. Mann-Whitney tests, ns: non-significant, *: p < 0.05, **: p < 0.01, ***: p < 0.001, ****: p < 0.0001.

Techniques: Expressing, Mutagenesis, Fluorescence, MANN-WHITNEY

Journal: bioRxiv

Article Title: βII and βIII spectrin paralogues define robustness and specialization of the neuronal membrane periodic skeleton

doi: 10.64898/2026.03.23.713115

Figure Lengend Snippet: a, b Representative d STORM images of wild-type and mutant βII-spectrins (a) and wild-type and mutant βIII-spectrins (b) imaged in re-expression condition in the indicated neuronal compartments. The non-periodic controls are the same as in . PSD95 was imaged using epifluorescence microscopy. Scale bars, 1 µm. c, d βII-spectrin (a) and βIII-spectrins (b) 1D autocorrelation amplitudes measured in the indicated compartments. n between 31 and 162 regions of interest per compartment obtained from 3 to 5 independent experiments for βII-spectrin. n between 73 and 213 regions of interest per compartment obtained from 3 to 4 independent experiments βIII-spectrins. Each box represents the median with percentile. Mann-Whitney tests, ns: non-significant, *: p < 0.05, **: p < 0.01, ****: p < 0.0001. e, f, Spacing between βII-spectrin (e) or βIII-spectrin (f) epitopes obtained from the same datasets as in (c) and (d).

Techniques: Mutagenesis, Expressing, Epifluorescence Microscopy, MANN-WHITNEY

Journal: bioRxiv

Article Title: βII and βIII spectrin paralogues define robustness and specialization of the neuronal membrane periodic skeleton

doi: 10.64898/2026.03.23.713115

Figure Lengend Snippet: a, Schematic of the periodic actin-spectrin cytoskeleton in axons (βII-spectrin mostly), dendrites and dendritic spines (random βII and βIII spectrins distribution with the presence of sparse βII/βIII heterotypic tetramers). Spectrin signals are excluded from post-synaptic densities. b, Schematic of βII- and βIII-spectrins sensitivity to their binding partners.

Techniques: Binding Assay

$( A to D ) Left: Stitched SIM images showing the distributions of endogenous endocytic pits, clathrin (A), Cav1 (B), Flot1 (C), or EndoA2 (D) in WT neurons. Endocytic pits are shown in green, with compartment markers MAP2 (magenta) and neurofacsin (yellow). Scale bar, 10 μm. Right: Enlarged SIM images of the three boxed regions on the left, corresponding to soma, dendrite, and AIS compartments, respectively. Scale bar, 2 μm. ( E ) Boxplots showing the area fraction of endogenous endocytic pits in different compartments of WT neurons. ( F ) Left: SIM images of tau (magenta) and endogenous endocytic pits (green) in distal axons of WT neurons. Right: The same as on the left, but in βII-spectrin KD neurons. Scale bars, 2 μm. ( G ) Boxplots showing the area fraction of endogenous endocytic pits (green) in distal axons of WT and βII-spectrin KD neurons. ( H ) Left: SIM images of MAP2 (magenta) and endogenous endocytic pits (green) in dendrites of WT neurons. Right: The same as on the left, but in βII-spectrin KD neurons. Scale bars, 2 μm. ( I ) Boxplots showing the area fraction of endogenous endocytic pits in dendrites of WT and βII-spectrin KD neurons.$

Journal: Science Advances

Article Title: Membrane-associated periodic skeleton regulates major forms of endocytosis in neurons through a signaling-driven positive feedback loop

doi: 10.1126/sciadv.aeb0803

Figure Lengend Snippet: ( A to D ) Left: Stitched SIM images showing the distributions of endogenous endocytic pits, clathrin (A), Cav1 (B), Flot1 (C), or EndoA2 (D) in WT neurons. Endocytic pits are shown in green, with compartment markers MAP2 (magenta) and neurofacsin (yellow). Scale bar, 10 μm. Right: Enlarged SIM images of the three boxed regions on the left, corresponding to soma, dendrite, and AIS compartments, respectively. Scale bar, 2 μm. ( E ) Boxplots showing the area fraction of endogenous endocytic pits in different compartments of WT neurons. ( F ) Left: SIM images of tau (magenta) and endogenous endocytic pits (green) in distal axons of WT neurons. Right: The same as on the left, but in βII-spectrin KD neurons. Scale bars, 2 μm. ( G ) Boxplots showing the area fraction of endogenous endocytic pits (green) in distal axons of WT and βII-spectrin KD neurons. ( H ) Left: SIM images of MAP2 (magenta) and endogenous endocytic pits (green) in dendrites of WT neurons. Right: The same as on the left, but in βII-spectrin KD neurons. Scale bars, 2 μm. ( I ) Boxplots showing the area fraction of endogenous endocytic pits in dendrites of WT and βII-spectrin KD neurons.

Article Snippet: The following primary antibodies were used in this study: guinea pig anti-tau antibody 1:500 dilution for IF (Synaptic Systems, 314004), mouse anti-tau antibody 1:500 dilution for IF (BD Biosciences, 556319), guinea pig anti-MAP2 antibody 1:500 dilution for IF (Synaptic Systems, 188004), rabbit anti-MAP2 antibody 1:500 dilution for IF (Synaptic Systems, 188002), chicken anti-neurofascin antibody (R&D system, AF3235), rabbit anti-CHC antibody 1:500 dilution for IF (Abcam, ab21679), rabbit anti-Cav1 antibody 1:400 dilution for IF (Cell Signaling Technology, 3238S), mouse anti-Flot1 antibody 1:100 dilution for IF (BD Biosciences, 610820), mouse anti-endophilinA2 antibody 1:100 dilution for IF (Santa Cruz Biotechnology, sc-365704), mouse anti–αII-spectrin (EnCor Biotechnology, MCA-3D7), mouse anti-βII spectrin antibody 1:200 dilution for IF (Santa Cruz Biotechnology, sc-515592), mouse anti-βII spectrin antibody 1:200 dilution for IF (BD Biosciences, 612563), rabbit anti-adducin antibody 1:500 dilution for IF (Abcam, ab51130), chicken anti-GFP antibody 1:500 dilution for IF (Thermo Fisher Scientific, A10262), rabbit anti-GFP antibody 1:500 dilution for IF (Thermo Fisher Scientific, A11122), goat anti-βIII spectrin antibody 1:100 dilution for IF (Santa Cruz Biotechnology, sc-9660), mouse anti-βIII spectrin antibody 1:100 dilution for IF (Santa Cruz Biotechnology, sc-515737), mouse anti-HA antibody 1:200 dilution for HA-mGluR5a internalization and IF (Thermo Fisher Scientific, 26183), rat anti-NCAM1 (CD56) antibody 1:40 dilution for NCAM1 internalization and IF (Cedarlane, CL10008AP), rat anti-TfR (CD71) antibody 1:500 dilution for IF (Bio-Rad, MCA1033GA), goat anti–LDL receptor (LDLR) antibody 1:100 dilution for IF (Thermo Fisher Scientific, PA5-46987), rabbit anti–phospho-ERK antibody 1:300 dilution (Cell Signaling Technology, 4370S), mouse anti-Aβ42 antibody 1:200 dilution for IF (BioLegend, 805501), and rabbit anti–cleaved caspase-3 (Asp175) antibody 1:400 dilution for IF (Cell Signaling Technology, 9661).

Techniques:

( A ) Schematic illustrating the spatial distributions of clathrin, Cav1, Flot1, and EndoA2 endocytic pits, relative to periodic MPS lattice in axons. ( B ) Schematic illustrating two distinct types of endocytic pits based on their spatial positioning relative to periodic βII-spectrin lattice in axons. Class I pits do not overlap with MPS lattice, whereas class II do. The MPS was visualized by immunostaining with antibodies targeting the C terminus of βII-spectrin, which mark the centers of spectrin tetramers. ( C ) The same as in (B) but showing spatial relationships with the periodic adducin lattice in axons. The MPS was visualized by immunostaining with antibodies targeting the adducin, which mark the terminal ends of spectrin tetramers. ( D ) Left: Dual-color STORM images of βII-spectrin (magenta) and endogenous clathrin (green) in axons. Right: Magnified views of class I and class II CCPs in the boxed regions. Scale bars, 10 μm (left), 5 μm (middle), and 200 nm (right). ( E ) PCCs between βII-spectrin and endogenous clathrin under experimental and randomized conditions. ( F ) Left: Averaged dual-color STORM images of βII-spectrin (magenta) and endogenous clathrin (green), generated by aligning individual STORM images to the centers of CCPs. Right: Radial intensity profiles of the averaged images shown on the left. Scale bar, 100 nm. ( G to I ) The same as in (D) to (F) but for βII-spectrin (magenta) and exogenously expressed Cav1 (green). ( J to L ) The same as in (D) to (F) but for adducin (magenta) and exogenously expressed Flot1 (green). ( M to O ) The same as in (D) to (F) but for adducin (magenta) and exogenously expressed EndoA2 (green). ( P ) Percentages of class I and class II pits for endogenous clathrin, exogenously expressed Cav1, exogenously expressed Flot1 and exogenously expressed EndoA2 in axons.

Journal: Science Advances

Article Title: Membrane-associated periodic skeleton regulates major forms of endocytosis in neurons through a signaling-driven positive feedback loop

doi: 10.1126/sciadv.aeb0803

Figure Lengend Snippet: ( A ) Schematic illustrating the spatial distributions of clathrin, Cav1, Flot1, and EndoA2 endocytic pits, relative to periodic MPS lattice in axons. ( B ) Schematic illustrating two distinct types of endocytic pits based on their spatial positioning relative to periodic βII-spectrin lattice in axons. Class I pits do not overlap with MPS lattice, whereas class II do. The MPS was visualized by immunostaining with antibodies targeting the C terminus of βII-spectrin, which mark the centers of spectrin tetramers. ( C ) The same as in (B) but showing spatial relationships with the periodic adducin lattice in axons. The MPS was visualized by immunostaining with antibodies targeting the adducin, which mark the terminal ends of spectrin tetramers. ( D ) Left: Dual-color STORM images of βII-spectrin (magenta) and endogenous clathrin (green) in axons. Right: Magnified views of class I and class II CCPs in the boxed regions. Scale bars, 10 μm (left), 5 μm (middle), and 200 nm (right). ( E ) PCCs between βII-spectrin and endogenous clathrin under experimental and randomized conditions. ( F ) Left: Averaged dual-color STORM images of βII-spectrin (magenta) and endogenous clathrin (green), generated by aligning individual STORM images to the centers of CCPs. Right: Radial intensity profiles of the averaged images shown on the left. Scale bar, 100 nm. ( G to I ) The same as in (D) to (F) but for βII-spectrin (magenta) and exogenously expressed Cav1 (green). ( J to L ) The same as in (D) to (F) but for adducin (magenta) and exogenously expressed Flot1 (green). ( M to O ) The same as in (D) to (F) but for adducin (magenta) and exogenously expressed EndoA2 (green). ( P ) Percentages of class I and class II pits for endogenous clathrin, exogenously expressed Cav1, exogenously expressed Flot1 and exogenously expressed EndoA2 in axons.

Techniques: Immunostaining, Generated

Journal: Science Advances

Article Title: Membrane-associated periodic skeleton regulates major forms of endocytosis in neurons through a signaling-driven positive feedback loop

doi: 10.1126/sciadv.aeb0803

Figure Lengend Snippet: ( A ) Schematic illustrating the spatial distribution of clathrin, Cav1, Flot1, and EndoA2 endocytic pits, relative to periodic MPS lattice in dendrites. ( B ) Schematic illustrating two distinct types of endocytic pits based on their spatial positioning relative to periodic βIII-spectrin or adducin lattice in dendrites. Class I pits do not overlap with MPS lattice, whereas class II pits do. The MPS was visualized by immunostaining with antibodies targeting the N terminus of βIII-spectrin or adducin, which both mark terminal ends of spectrin tetramers. ( C ) Left: Dual-color STORM images of βIII-spectrin (magenta) and endogenous clathrin (green) in dendrites. Right: Magnified views of class I and class II CCPs in the boxed regions. Scale bars, 10 μm (left), 5 μm (middle), 200 nm (right). ( D ) PCCs between βIII-spectrin and endogenous clathrin under experimental and randomized conditions. ( E ) Left: Averaged dual-color STROM images of βIII-spectrin (magenta) and endogenous clathrin (green), generated by aligning individual STORM images to the centers of CCPs. Right: Radial intensity profile of averaged images shown on the left. Scale bar, 100 nm. ( F to H ) The same as in (C) to (E) but for adducin (magenta) and exogenously expressed Cav1 (green). ( I to K ) The same as in (C) to (E) but for adducin (magenta) and exogenously expressed Flot1 (green). ( L to N ) The same as in (C) to (E) but for adducin (magenta) and exogenously expressed EndoA2 (green). ( O ) Percentages of class I and class II endocytic pits for endogenous clathrin, exogenously expressed Cav1, exogenously expressed Flot1, and exogenously expressed EndoA2 in dendrites.

Techniques: Immunostaining, Generated

$( A ) Confocal fluorescence images of MAP2 (magenta) and internalized CF568-transferrin (green) in somatodendritic region of WT or βII-spectrin KD neurons treated with CF568-transferrin for 2, 10, and 20 min. Scale bars, 10 μm. ( B ) Time course of CF568-transferrin endocytosis in somatodendritic regions of WT and βII-spectrin KD neurons, quantified by the area fraction of transferrin-positive endosomes. Solid lines represent single-exponential fits to the data. ( C ) Confocal fluorescence images of MAP2 (gray), internalized HA-mGluR5a (green), and endogenous Cav1 (magenta) in somatodendritic region of WT or βII-spectrin KD neurons overexpressing HA-mGluR5a and treated with anti-HA antibody for 5, 10, and 20 min. Scale bars, 10 μm. ( D ) Time course of Cav1-mediated HA-mGluR5a endocytosis in the somatodendritic regions of WT and βII-spectrin KD neurons, quantified by the area fraction of Cav1-positive HA-mGluR5a endosomes. Solid lines represent single-exponential fits to the data. ( E ) SIM images of internalized NCAM1 (green) and endogenous EndoA2 (magenta) in axonal (top) and somatodendritic (bottom) regions of WT or βII-spectrin KD neurons treated with anti-NCAM1 antibody for 30 min. Scale bars, 2 μm. ( F ) Boxplots of EndoA2-mediated NCAM1 endocytosis in axonal and somatodendritic regions of WT and βII-spectrin KD neurons, quantified by the area proportion of EndoA2-positive NCAM1 endosomes.$

Journal: Science Advances

Article Title: Membrane-associated periodic skeleton regulates major forms of endocytosis in neurons through a signaling-driven positive feedback loop

doi: 10.1126/sciadv.aeb0803

Figure Lengend Snippet: ( A ) Confocal fluorescence images of MAP2 (magenta) and internalized CF568-transferrin (green) in somatodendritic region of WT or βII-spectrin KD neurons treated with CF568-transferrin for 2, 10, and 20 min. Scale bars, 10 μm. ( B ) Time course of CF568-transferrin endocytosis in somatodendritic regions of WT and βII-spectrin KD neurons, quantified by the area fraction of transferrin-positive endosomes. Solid lines represent single-exponential fits to the data. ( C ) Confocal fluorescence images of MAP2 (gray), internalized HA-mGluR5a (green), and endogenous Cav1 (magenta) in somatodendritic region of WT or βII-spectrin KD neurons overexpressing HA-mGluR5a and treated with anti-HA antibody for 5, 10, and 20 min. Scale bars, 10 μm. ( D ) Time course of Cav1-mediated HA-mGluR5a endocytosis in the somatodendritic regions of WT and βII-spectrin KD neurons, quantified by the area fraction of Cav1-positive HA-mGluR5a endosomes. Solid lines represent single-exponential fits to the data. ( E ) SIM images of internalized NCAM1 (green) and endogenous EndoA2 (magenta) in axonal (top) and somatodendritic (bottom) regions of WT or βII-spectrin KD neurons treated with anti-NCAM1 antibody for 30 min. Scale bars, 2 μm. ( F ) Boxplots of EndoA2-mediated NCAM1 endocytosis in axonal and somatodendritic regions of WT and βII-spectrin KD neurons, quantified by the area proportion of EndoA2-positive NCAM1 endosomes.

Techniques: Fluorescence

$( A ) Schematic illustrating ligand-induced ERK activation via three major endocytic pathways: CME of TfR, LRME of HA-mGluR5a, and FEME of NCAM1. ( B ) Top: Epi-fluorescence images showing pERK immunostaining in neurons without ligand treatment, neurons treated with CF568-transferrin, and neurons overexpressing HA-mGluR5a treated with anti-HA antibody. Bottom: The same as the top but with neurons pretreated with dyngo-4a before ligand treatment. Scale bars, 25 μm. ( C ) Time course of ERK activation in neurons under the same conditions as in (B). ( D ) 3D STORM images of immunostained βIII-spectrin in dendrites of neurons under various treatments. First column: neurons pretreated with dimethyl sulfoxide (DMSO), dyngo-4a, U0126, MDL, or VAD. Second column: neurons pretreated with the same inhibitors followed by CF568-transferrin treatment. Third column: neurons overexpressing HA-mGluR5a pretreated with the same inhibitors followed by the anti-HA antibody treatment. Fourth column: neurons pretreated with the same inhibitors followed by anti-NCAM1 antibody treatment. Scale bars, 1 μm. Color scale bar represents the z -coordinate information. ( E ) Averaged 1D autocorrelation amplitudes of βIII-spectrin, calculated for the same conditions as in (D). ( F ) SIM images of MAP2 (magenta) and internalized CF568-transferrin (green) in neurons pretreated with DMSO, MDL, or VAD followed by CF568-transferrin treatment. Scale bars, 2 μm. ( G ) Boxplots of transferrin-positive endosome area fractions. ( H ) Confocal fluorescence images of MAP2 (magenta) and internalized HA-mGluR5a (green) in neurons overexpressing HA-mGluR5a pretreated with DMSO, MDL, or VAD followed by anti-HA antibody treatment. Scale bars, 10 μm. ( I ) Boxplots of HA-mGluR5a endosome area fractions. ( J ) Schematic summarizing the proposed positive feedback mechanism: Receptor endocytosis via CME, LRME, or FEME activates ERK signaling, which triggers calpain- and caspase-mediated MPS degradation; MPS disruption in turn facilitates further endocytosis, establishing a positive feedback loop.$

Journal: Science Advances

Article Title: Membrane-associated periodic skeleton regulates major forms of endocytosis in neurons through a signaling-driven positive feedback loop

doi: 10.1126/sciadv.aeb0803

Figure Lengend Snippet: ( A ) Schematic illustrating ligand-induced ERK activation via three major endocytic pathways: CME of TfR, LRME of HA-mGluR5a, and FEME of NCAM1. ( B ) Top: Epi-fluorescence images showing pERK immunostaining in neurons without ligand treatment, neurons treated with CF568-transferrin, and neurons overexpressing HA-mGluR5a treated with anti-HA antibody. Bottom: The same as the top but with neurons pretreated with dyngo-4a before ligand treatment. Scale bars, 25 μm. ( C ) Time course of ERK activation in neurons under the same conditions as in (B). ( D ) 3D STORM images of immunostained βIII-spectrin in dendrites of neurons under various treatments. First column: neurons pretreated with dimethyl sulfoxide (DMSO), dyngo-4a, U0126, MDL, or VAD. Second column: neurons pretreated with the same inhibitors followed by CF568-transferrin treatment. Third column: neurons overexpressing HA-mGluR5a pretreated with the same inhibitors followed by the anti-HA antibody treatment. Fourth column: neurons pretreated with the same inhibitors followed by anti-NCAM1 antibody treatment. Scale bars, 1 μm. Color scale bar represents the z -coordinate information. ( E ) Averaged 1D autocorrelation amplitudes of βIII-spectrin, calculated for the same conditions as in (D). ( F ) SIM images of MAP2 (magenta) and internalized CF568-transferrin (green) in neurons pretreated with DMSO, MDL, or VAD followed by CF568-transferrin treatment. Scale bars, 2 μm. ( G ) Boxplots of transferrin-positive endosome area fractions. ( H ) Confocal fluorescence images of MAP2 (magenta) and internalized HA-mGluR5a (green) in neurons overexpressing HA-mGluR5a pretreated with DMSO, MDL, or VAD followed by anti-HA antibody treatment. Scale bars, 10 μm. ( I ) Boxplots of HA-mGluR5a endosome area fractions. ( J ) Schematic summarizing the proposed positive feedback mechanism: Receptor endocytosis via CME, LRME, or FEME activates ERK signaling, which triggers calpain- and caspase-mediated MPS degradation; MPS disruption in turn facilitates further endocytosis, establishing a positive feedback loop.

Techniques: Activation Assay, Fluorescence, Immunostaining, Disruption

$( A ) Schematic illustrating the sequential cleavage of APP695 by β-secretase and γ-secretase to produce Aβ42. ( B ) Schematic illustrating the structure of SEP-APP. ( C ) Left: Epi-fluorescence images of pERK in neurons overexpressing SEP-APP without ligand treatment. Middle: The same as the left but treated with GFP nanobody. Right: The same as the middle but with dyngo-4a preincubation before GFP nanobody treatment. Scale bars, 25 μm. ( D ) Time course of ERK activation in neurons under the same conditions as in (C). ( E ) 3D STORM images of immunostained βIII-spectrin in dendrites of neurons pretreated with DMSO, dyngo-4a, U0126, MDL, or VAD followed by GFP nanobody treatment. Scale bars, 1 μm. ( F ) Averaged 1D autocorrelation amplitude of βIII-spectrin, calculated for the same conditions as in (E). ( G ) Confocal fluorescence images of CTB (magenta) and internalized SEP-APP (green) in neurons pretreated with DMSO, MDL, or VAD followed by GFP nanobody treatment. Scale bars, 10 μm. ( H ) Boxplots of SEP-APP endosome area fractions. ( I ) Left: Confocal fluorescence images of MAP2 (magenta) and intracellular Aβ42 (green) in WT neurons, neurons overexpressing APPwt, and neurons overexpressing APPswe. Right: The same as the left but in βII-spectrin KD neurons. Scale bars, 10 μm. ( J ) Boxplots of intracellular Aβ42 area fractions in somatodendritic regions of neurons. ( K ) Left, SIM images of MAP2 (magenta) and cleaved caspase-3 (green) in WT neurons, neurons overexpressing APPwt, and neurons overexpressing APPswe. Right: The same as the left but in βII-spectrin KD neurons. Scale bars, 2 μm. ( L ) Boxplots of cleaved caspase-3 area fractions in dendrites of neurons. ( M ) Schematic illustrating APP endocytosis triggers downstream ERK signaling, leading to MPS degradation through caspase- and calpain-mediated spectrin cleavage. This degradation further accelerates APP endocytosis, promoting intracellular Aβ42 accumulation and caspase-3 activation.$

Journal: Science Advances

Article Title: Membrane-associated periodic skeleton regulates major forms of endocytosis in neurons through a signaling-driven positive feedback loop

doi: 10.1126/sciadv.aeb0803

Figure Lengend Snippet: ( A ) Schematic illustrating the sequential cleavage of APP695 by β-secretase and γ-secretase to produce Aβ42. ( B ) Schematic illustrating the structure of SEP-APP. ( C ) Left: Epi-fluorescence images of pERK in neurons overexpressing SEP-APP without ligand treatment. Middle: The same as the left but treated with GFP nanobody. Right: The same as the middle but with dyngo-4a preincubation before GFP nanobody treatment. Scale bars, 25 μm. ( D ) Time course of ERK activation in neurons under the same conditions as in (C). ( E ) 3D STORM images of immunostained βIII-spectrin in dendrites of neurons pretreated with DMSO, dyngo-4a, U0126, MDL, or VAD followed by GFP nanobody treatment. Scale bars, 1 μm. ( F ) Averaged 1D autocorrelation amplitude of βIII-spectrin, calculated for the same conditions as in (E). ( G ) Confocal fluorescence images of CTB (magenta) and internalized SEP-APP (green) in neurons pretreated with DMSO, MDL, or VAD followed by GFP nanobody treatment. Scale bars, 10 μm. ( H ) Boxplots of SEP-APP endosome area fractions. ( I ) Left: Confocal fluorescence images of MAP2 (magenta) and intracellular Aβ42 (green) in WT neurons, neurons overexpressing APPwt, and neurons overexpressing APPswe. Right: The same as the left but in βII-spectrin KD neurons. Scale bars, 10 μm. ( J ) Boxplots of intracellular Aβ42 area fractions in somatodendritic regions of neurons. ( K ) Left, SIM images of MAP2 (magenta) and cleaved caspase-3 (green) in WT neurons, neurons overexpressing APPwt, and neurons overexpressing APPswe. Right: The same as the left but in βII-spectrin KD neurons. Scale bars, 2 μm. ( L ) Boxplots of cleaved caspase-3 area fractions in dendrites of neurons. ( M ) Schematic illustrating APP endocytosis triggers downstream ERK signaling, leading to MPS degradation through caspase- and calpain-mediated spectrin cleavage. This degradation further accelerates APP endocytosis, promoting intracellular Aβ42 accumulation and caspase-3 activation.

Techniques: Fluorescence, Activation Assay

Journal: Science Advances

Article Title: Membrane-associated periodic skeleton regulates major forms of endocytosis in neurons through a signaling-driven positive feedback loop

doi: 10.1126/sciadv.aeb0803

Techniques:

Journal: Science Advances

Article Title: Membrane-associated periodic skeleton regulates major forms of endocytosis in neurons through a signaling-driven positive feedback loop

doi: 10.1126/sciadv.aeb0803

Techniques: Immunostaining, Generated

Journal: Science Advances

Article Title: Membrane-associated periodic skeleton regulates major forms of endocytosis in neurons through a signaling-driven positive feedback loop

doi: 10.1126/sciadv.aeb0803

Techniques: Immunostaining, Generated

Journal: Science Advances

Article Title: Membrane-associated periodic skeleton regulates major forms of endocytosis in neurons through a signaling-driven positive feedback loop

doi: 10.1126/sciadv.aeb0803

Techniques: Fluorescence

Journal: Science Advances

Article Title: Membrane-associated periodic skeleton regulates major forms of endocytosis in neurons through a signaling-driven positive feedback loop

doi: 10.1126/sciadv.aeb0803

Techniques: Activation Assay, Fluorescence, Immunostaining, Disruption

Journal: Science Advances

Article Title: Membrane-associated periodic skeleton regulates major forms of endocytosis in neurons through a signaling-driven positive feedback loop

doi: 10.1126/sciadv.aeb0803

Techniques: Fluorescence, Activation Assay

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