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arpc5l (Proteintech)

Name: arpc5l
Brand: Proteintech
Rating: 93 (6 reviews)

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Proteintech arpc5l

SPIN90 selectively activates <t>ArpC5L</t> containing Arp2/3 complexes (A) SPIN90 efficiently activates ArpC5L but not ArpC5 containing Arp2/3 complexes. Representative plots of pyrene-actin polymerization assays with 10 nM Arp2/3 complex, 100 nM SPIN90 and 2.5 µM actin (5 % pyrene labelled). It demonstrates that ArpC5L- but not ArpC5-containing Arp2/3 complexes activated by SPIN90 induce rapid actin polymerization, regardless of the ArpC1 isoform. The experiments were repeated independently three times and yielded similar results. (B) Representative TIRF images demonstrate that ArpC5L- but not ArpC5-containing complex activated by SPIN90 efficiently generate actin filaments. Scale bar = 20 µm A mixture of 20 nM Arp2/3 complex, 200 nM SPIN90 and 0.5 µM actin (15 % Alexa 488 labelled) was observed overtime. The graph shows quantitative analysis of filament density over time from three independent technical replicates. The points indicate the mean density, and the error bars represent the standard deviation.

Arpc5l, supplied by Proteintech, used in various techniques. Bioz Stars score: 93/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/arpc5l/product/Proteintech
Average 93 stars, based on 6 article reviews

arpc5l - by Bioz Stars, 2026-02

93/100 stars

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1) Product Images from "SPIN90 modulates the architecture of lamellipodial actin in an ARPC5L dependent fashion"

Article Title: SPIN90 modulates the architecture of lamellipodial actin in an ARPC5L dependent fashion

Journal: bioRxiv

doi: 10.64898/2025.12.01.691495

SPIN90 selectively activates ArpC5L containing Arp2/3 complexes (A) SPIN90 efficiently activates ArpC5L but not ArpC5 containing Arp2/3 complexes. Representative plots of pyrene-actin polymerization assays with 10 nM Arp2/3 complex, 100 nM SPIN90 and 2.5 µM actin (5 % pyrene labelled). It demonstrates that ArpC5L- but not ArpC5-containing Arp2/3 complexes activated by SPIN90 induce rapid actin polymerization, regardless of the ArpC1 isoform. The experiments were repeated independently three times and yielded similar results. (B) Representative TIRF images demonstrate that ArpC5L- but not ArpC5-containing complex activated by SPIN90 efficiently generate actin filaments. Scale bar = 20 µm A mixture of 20 nM Arp2/3 complex, 200 nM SPIN90 and 0.5 µM actin (15 % Alexa 488 labelled) was observed overtime. The graph shows quantitative analysis of filament density over time from three independent technical replicates. The points indicate the mean density, and the error bars represent the standard deviation.

Figure Legend Snippet: SPIN90 selectively activates ArpC5L containing Arp2/3 complexes (A) SPIN90 efficiently activates ArpC5L but not ArpC5 containing Arp2/3 complexes. Representative plots of pyrene-actin polymerization assays with 10 nM Arp2/3 complex, 100 nM SPIN90 and 2.5 µM actin (5 % pyrene labelled). It demonstrates that ArpC5L- but not ArpC5-containing Arp2/3 complexes activated by SPIN90 induce rapid actin polymerization, regardless of the ArpC1 isoform. The experiments were repeated independently three times and yielded similar results. (B) Representative TIRF images demonstrate that ArpC5L- but not ArpC5-containing complex activated by SPIN90 efficiently generate actin filaments. Scale bar = 20 µm A mixture of 20 nM Arp2/3 complex, 200 nM SPIN90 and 0.5 µM actin (15 % Alexa 488 labelled) was observed overtime. The graph shows quantitative analysis of filament density over time from three independent technical replicates. The points indicate the mean density, and the error bars represent the standard deviation.

Techniques Used: Standard Deviation

SPIN90 has a higher affinity for Arp2/3 complexes with ArpC5L than ArpC5 (A) Surface representation of the Arp2/3 complex from the SPIN90-Arp2/3 complex structure (PDB: 6DEC). Residues in Arp2/3 complex subunits contacting the two SPIN90 molecules are shown in darker colours. (B) Immunoblots using an ArpC2 antibody show the amount of Arp2/3 complex containing ArpC1B pulled down with GST–SPIN90-Cter. Both blots were run on the same gel and developed on the same membrane to allow a direct comparison of signal intensity. (C) The graph shows the quantification of average normalized ArpC2 intensity from three independent replicates, with error bars resenting standard deviation. The data was fit with Hill equation.

Figure Legend Snippet: SPIN90 has a higher affinity for Arp2/3 complexes with ArpC5L than ArpC5 (A) Surface representation of the Arp2/3 complex from the SPIN90-Arp2/3 complex structure (PDB: 6DEC). Residues in Arp2/3 complex subunits contacting the two SPIN90 molecules are shown in darker colours. (B) Immunoblots using an ArpC2 antibody show the amount of Arp2/3 complex containing ArpC1B pulled down with GST–SPIN90-Cter. Both blots were run on the same gel and developed on the same membrane to allow a direct comparison of signal intensity. (C) The graph shows the quantification of average normalized ArpC2 intensity from three independent replicates, with error bars resenting standard deviation. The data was fit with Hill equation.

Techniques Used: Western Blot, Membrane, Comparison, Standard Deviation

SPIN90 localizes at the leading edge and integrates into lamellipodial actin networks. (A) Quantitative immunoblot analysis of endogenous levels of ArpC5 isoforms in B16 cells using recombinant His-tagged ArpC5 and His-tagged ArpC5L as standards. The average concentrations and standard deviations from three independent replicates are shown in the table on the right. (B) Schematic shows the two Ruby-tagged SPIN90 constructs expressed in cells. Representative live images show B16 cells overexpressing GFP (volume marker) together with Ruby–SPIN90 (upper) or with Ruby-SPIN90 Nter (lower). Scale bars = 5 µm. Signal intensity (right) is quantified by normalizing the intensity at the leading edge (solid line) compared to that 2□µm from the leading edge (dashed line). Each pair of points represents measurements from the same cell with the different colours representing data from three independent replicates. A two-tailed paired t-test is used to estimate the p-value.

Figure Legend Snippet: SPIN90 localizes at the leading edge and integrates into lamellipodial actin networks. (A) Quantitative immunoblot analysis of endogenous levels of ArpC5 isoforms in B16 cells using recombinant His-tagged ArpC5 and His-tagged ArpC5L as standards. The average concentrations and standard deviations from three independent replicates are shown in the table on the right. (B) Schematic shows the two Ruby-tagged SPIN90 constructs expressed in cells. Representative live images show B16 cells overexpressing GFP (volume marker) together with Ruby–SPIN90 (upper) or with Ruby-SPIN90 Nter (lower). Scale bars = 5 µm. Signal intensity (right) is quantified by normalizing the intensity at the leading edge (solid line) compared to that 2□µm from the leading edge (dashed line). Each pair of points represents measurements from the same cell with the different colours representing data from three independent replicates. A two-tailed paired t-test is used to estimate the p-value.

Techniques Used: Western Blot, Recombinant, Construct, Marker, Two Tailed Test

SPIN90 integrates into the lamellipodia with Arp2/3 complex (A) Representative maximum intensity projection over 14 seconds for cells expressing endogenous NeonGreen–ArpC5L, together with overexpressed Ruby–SPIN90 or Ruby–SPIN90-Nter. ArpC5L and Ruby–SPIN90, but not Ruby–SPIN90-Nter undergo rearward movement in the lamellipodium (highlighted with yellow arrows). The similar trajectory pattern observed in all the cells (20 for SPIN90-FL and 13 for SPIN90-Nter) across three independent replicates. (B) Representative live image (upper) of B16 cells with endogenously labelled NeonGreen-ArpC5L and overexpressing Ruby–SPIN90. Kymographs (lower), generated from the orange lines in the upper images, show that ArpC5L (left) and SPIN90 (right) exhibit directional movement, highlighted with blue arrows. Quantitative analysis (right panel) of the rearward flow of ArpC5L and SPIN90 respectively. Different colours indicate results from three independent replicates. A two-tailed unpaired t-test with Welsh’s correction is used to estimate the p-value. Scale bars = 5 µm

Figure Legend Snippet: SPIN90 integrates into the lamellipodia with Arp2/3 complex (A) Representative maximum intensity projection over 14 seconds for cells expressing endogenous NeonGreen–ArpC5L, together with overexpressed Ruby–SPIN90 or Ruby–SPIN90-Nter. ArpC5L and Ruby–SPIN90, but not Ruby–SPIN90-Nter undergo rearward movement in the lamellipodium (highlighted with yellow arrows). The similar trajectory pattern observed in all the cells (20 for SPIN90-FL and 13 for SPIN90-Nter) across three independent replicates. (B) Representative live image (upper) of B16 cells with endogenously labelled NeonGreen-ArpC5L and overexpressing Ruby–SPIN90. Kymographs (lower), generated from the orange lines in the upper images, show that ArpC5L (left) and SPIN90 (right) exhibit directional movement, highlighted with blue arrows. Quantitative analysis (right panel) of the rearward flow of ArpC5L and SPIN90 respectively. Different colours indicate results from three independent replicates. A two-tailed unpaired t-test with Welsh’s correction is used to estimate the p-value. Scale bars = 5 µm

Techniques Used: Expressing, Generated, Two Tailed Test

SPIN90 enhances the recruitment of ArpC5L but not ArpC5 to the leading edge Representative images of live cells expressing endogenous NeonGreen–ArpC5L (A) or ArpC5-NeonGreen (B) after treatment with the indicated siRNAs. Allstar represents siRNA control. The graphs show quantification of the ArpC5L or ArpC5 signal intensity at the leading edge in the different conditions. Each point represents an individual cell, with different colours indicating 3 independent experimental replicates. For each repeat, 8-15 cells were imaged and quantified. The mean of each experiment is shown as a circle, and error bars are standard deviation. A two-tailed paired t-test was used to calculate the p-value. Scale bars = 5 µm

Figure Legend Snippet: SPIN90 enhances the recruitment of ArpC5L but not ArpC5 to the leading edge Representative images of live cells expressing endogenous NeonGreen–ArpC5L (A) or ArpC5-NeonGreen (B) after treatment with the indicated siRNAs. Allstar represents siRNA control. The graphs show quantification of the ArpC5L or ArpC5 signal intensity at the leading edge in the different conditions. Each point represents an individual cell, with different colours indicating 3 independent experimental replicates. For each repeat, 8-15 cells were imaged and quantified. The mean of each experiment is shown as a circle, and error bars are standard deviation. A two-tailed paired t-test was used to calculate the p-value. Scale bars = 5 µm

Techniques Used: Expressing, Control, Standard Deviation, Two Tailed Test

The organisation of actin filaments at the leading edge of B16 cells. (A) Schematic representation of ρ (rho) and ψ (psi) in the organization of the actin network. (B) Representative images of an Alexa-488 phalloidin stained B16 cell for each cell line as indicated. The coloured region in the lamellipodium is the result of polarimetry analysis within a 0.65 µm (10-pixel) region from the leading edge to determine the mean actin filament orientation in each pixel. The mean filament orientation per pixel is represented with a stick whose orientation corresponds to filament orientation (angle rho, ρ) and whose color depicts filament orientation with respect to the leading edge (angle rho c , ρ c ) within the 0–180° range according to the colour bar. The stick maps of a representative ROI (labelled with white rectangles) are zoomed in and shown. (C) The polar histogram shows the statistical distribution of actin filament angles (ρ c ) per pixel within the 0–90° range relative to the leading edge of all the cells, with 38 to 55 cells analysed per condition across three independent repeats. The average < ρ c > and standard deviation for each cell line are indicated. The colours correspond to the colour bar shown in panel A. (D) Violin plot showing the statistical distribution of actin filament angles (ρ c ) per pixel within the 0–90° range, as shown in panel B. A two-tailed Mann–Whitney test was used to calculate the p-value between individual cells under two conditions. The medians and interquartile ranges are shown as black lines, while the means and standard deviations are shown as blue dots with error bars. (E) The statistical results of the average lamellipodial actin filament angle < ρ c > relative to the leading edge within the 0–90° range in individual wildtype, ArpC5, ArpC5Lor SPIN90 knockout cells. Each point represents the mean angle of actin filaments relative to the leading edge in a single cell from three independent experiments, the latter shown in different colours. Mean ± SD for each experimental condition is indicated. A two-tailed Welch’s t-test is used to estimate the p-value between the means under two conditions. (F) The statistical results of the standard deviation (SD) of actin filament angles relative to the leading edge within the 0–90° range in individual wildtype, ArpC5, ArpC5L, or SPIN90 knockout cells. Each point represents the SD of actin filaments relative to the leading edge in a single cell from three independent experiments, the latter shown in different colours. Mean ± SD for each experimental condition is indicated. A two-tailed Mann Whitney test is used to estimate the p-value between individual cells under two conditions. (G) Representative images of Alexa-488 phalloidin stained B16 cell (right) overexpressing Ruby-SPIN90 (left). The zoomed-in image shows the mean actin filament orientation per pixel within the ROI (white rectangle) as in panel A. (H) The polar histogram shows the statistical distribution of actin filament angles (ρ c ) per pixel within the 0–90° range relative to the leading edge in all cells overexpressing either Ruby-SPIN90 (61 cells) or Ruby-SPIN90 Nter (59 cells), across three independent experimental repeats. The average < ρ c > and standard deviation for each experimental condition are indicated. The colours correspond to the colour bar shown in panel A.

Figure Legend Snippet: The organisation of actin filaments at the leading edge of B16 cells. (A) Schematic representation of ρ (rho) and ψ (psi) in the organization of the actin network. (B) Representative images of an Alexa-488 phalloidin stained B16 cell for each cell line as indicated. The coloured region in the lamellipodium is the result of polarimetry analysis within a 0.65 µm (10-pixel) region from the leading edge to determine the mean actin filament orientation in each pixel. The mean filament orientation per pixel is represented with a stick whose orientation corresponds to filament orientation (angle rho, ρ) and whose color depicts filament orientation with respect to the leading edge (angle rho c , ρ c ) within the 0–180° range according to the colour bar. The stick maps of a representative ROI (labelled with white rectangles) are zoomed in and shown. (C) The polar histogram shows the statistical distribution of actin filament angles (ρ c ) per pixel within the 0–90° range relative to the leading edge of all the cells, with 38 to 55 cells analysed per condition across three independent repeats. The average < ρ c > and standard deviation for each cell line are indicated. The colours correspond to the colour bar shown in panel A. (D) Violin plot showing the statistical distribution of actin filament angles (ρ c ) per pixel within the 0–90° range, as shown in panel B. A two-tailed Mann–Whitney test was used to calculate the p-value between individual cells under two conditions. The medians and interquartile ranges are shown as black lines, while the means and standard deviations are shown as blue dots with error bars. (E) The statistical results of the average lamellipodial actin filament angle < ρ c > relative to the leading edge within the 0–90° range in individual wildtype, ArpC5, ArpC5Lor SPIN90 knockout cells. Each point represents the mean angle of actin filaments relative to the leading edge in a single cell from three independent experiments, the latter shown in different colours. Mean ± SD for each experimental condition is indicated. A two-tailed Welch’s t-test is used to estimate the p-value between the means under two conditions. (F) The statistical results of the standard deviation (SD) of actin filament angles relative to the leading edge within the 0–90° range in individual wildtype, ArpC5, ArpC5L, or SPIN90 knockout cells. Each point represents the SD of actin filaments relative to the leading edge in a single cell from three independent experiments, the latter shown in different colours. Mean ± SD for each experimental condition is indicated. A two-tailed Mann Whitney test is used to estimate the p-value between individual cells under two conditions. (G) Representative images of Alexa-488 phalloidin stained B16 cell (right) overexpressing Ruby-SPIN90 (left). The zoomed-in image shows the mean actin filament orientation per pixel within the ROI (white rectangle) as in panel A. (H) The polar histogram shows the statistical distribution of actin filament angles (ρ c ) per pixel within the 0–90° range relative to the leading edge in all cells overexpressing either Ruby-SPIN90 (61 cells) or Ruby-SPIN90 Nter (59 cells), across three independent experimental repeats. The average < ρ c > and standard deviation for each experimental condition are indicated. The colours correspond to the colour bar shown in panel A.

Techniques Used: Staining, Standard Deviation, Two Tailed Test, MANN-WHITNEY, Knock-Out

Schematic summary (A) In migrating cells, SPIN90 recruits the ArpC5L-, but not the ArpC5-containing complex, to the lamellipodial leading edge . Meanwhile, both ArpC5L- and ArpC5-containing complexes generate branches at the lamellipodia . Thus, SPIN90 and Arp2/3 iso-complexes integrate into the lamellipodial actin network, contributing to the formation of a complex actin architecture that ensures efficient protrusion . (B) ArpC5 KO cells (left panel), the ArpC5L-containing complex participates in the formation of both linear and branched actin filaments. Consequently, the distribution of filament orientations in their lamellipodia is much fig than that of the wild type. In contrast, in ArpC5L KO cells (right panel), the ArpC5-containing complex generates only branched actin filaments, resulting in a narrower distribution of filament orientations.

Figure Legend Snippet: Schematic summary (A) In migrating cells, SPIN90 recruits the ArpC5L-, but not the ArpC5-containing complex, to the lamellipodial leading edge . Meanwhile, both ArpC5L- and ArpC5-containing complexes generate branches at the lamellipodia . Thus, SPIN90 and Arp2/3 iso-complexes integrate into the lamellipodial actin network, contributing to the formation of a complex actin architecture that ensures efficient protrusion . (B) ArpC5 KO cells (left panel), the ArpC5L-containing complex participates in the formation of both linear and branched actin filaments. Consequently, the distribution of filament orientations in their lamellipodia is much fig than that of the wild type. In contrast, in ArpC5L KO cells (right panel), the ArpC5-containing complex generates only branched actin filaments, resulting in a narrower distribution of filament orientations.

Techniques Used:

Image Search Results

Journal: bioRxiv

Article Title: SPIN90 modulates the architecture of lamellipodial actin in an ARPC5L dependent fashion

doi: 10.64898/2025.12.01.691495

Figure Lengend Snippet: SPIN90 selectively activates ArpC5L containing Arp2/3 complexes (A) SPIN90 efficiently activates ArpC5L but not ArpC5 containing Arp2/3 complexes. Representative plots of pyrene-actin polymerization assays with 10 nM Arp2/3 complex, 100 nM SPIN90 and 2.5 µM actin (5 % pyrene labelled). It demonstrates that ArpC5L- but not ArpC5-containing Arp2/3 complexes activated by SPIN90 induce rapid actin polymerization, regardless of the ArpC1 isoform. The experiments were repeated independently three times and yielded similar results. (B) Representative TIRF images demonstrate that ArpC5L- but not ArpC5-containing complex activated by SPIN90 efficiently generate actin filaments. Scale bar = 20 µm A mixture of 20 nM Arp2/3 complex, 200 nM SPIN90 and 0.5 µM actin (15 % Alexa 488 labelled) was observed overtime. The graph shows quantitative analysis of filament density over time from three independent technical replicates. The points indicate the mean density, and the error bars represent the standard deviation.

Article Snippet: Other antibodies are including: ARPC2/p34-Arc polyclonal (Millipore, 07-227), ARPC5 monoclonal (Synaptic Systems, 305011), ArpC5L (Proteintech, 22025-a-AP), β-actin (Abcam, ab179467), anti-mouse IgG-IRDye® 800CW (LI-COR Biosciences, 926-32210) and anti-rabbit IgG-IRDye® 680RD (LI-COR Biosciences, 926-68071).

Techniques: Standard Deviation

Journal: bioRxiv

Article Title: SPIN90 modulates the architecture of lamellipodial actin in an ARPC5L dependent fashion

doi: 10.64898/2025.12.01.691495

Figure Lengend Snippet: SPIN90 has a higher affinity for Arp2/3 complexes with ArpC5L than ArpC5 (A) Surface representation of the Arp2/3 complex from the SPIN90-Arp2/3 complex structure (PDB: 6DEC). Residues in Arp2/3 complex subunits contacting the two SPIN90 molecules are shown in darker colours. (B) Immunoblots using an ArpC2 antibody show the amount of Arp2/3 complex containing ArpC1B pulled down with GST–SPIN90-Cter. Both blots were run on the same gel and developed on the same membrane to allow a direct comparison of signal intensity. (C) The graph shows the quantification of average normalized ArpC2 intensity from three independent replicates, with error bars resenting standard deviation. The data was fit with Hill equation.

Techniques: Western Blot, Membrane, Comparison, Standard Deviation

Journal: bioRxiv

Article Title: SPIN90 modulates the architecture of lamellipodial actin in an ARPC5L dependent fashion

doi: 10.64898/2025.12.01.691495

Figure Lengend Snippet: SPIN90 localizes at the leading edge and integrates into lamellipodial actin networks. (A) Quantitative immunoblot analysis of endogenous levels of ArpC5 isoforms in B16 cells using recombinant His-tagged ArpC5 and His-tagged ArpC5L as standards. The average concentrations and standard deviations from three independent replicates are shown in the table on the right. (B) Schematic shows the two Ruby-tagged SPIN90 constructs expressed in cells. Representative live images show B16 cells overexpressing GFP (volume marker) together with Ruby–SPIN90 (upper) or with Ruby-SPIN90 Nter (lower). Scale bars = 5 µm. Signal intensity (right) is quantified by normalizing the intensity at the leading edge (solid line) compared to that 2□µm from the leading edge (dashed line). Each pair of points represents measurements from the same cell with the different colours representing data from three independent replicates. A two-tailed paired t-test is used to estimate the p-value.

Techniques: Western Blot, Recombinant, Construct, Marker, Two Tailed Test

Journal: bioRxiv

Article Title: SPIN90 modulates the architecture of lamellipodial actin in an ARPC5L dependent fashion

doi: 10.64898/2025.12.01.691495

Figure Lengend Snippet: SPIN90 integrates into the lamellipodia with Arp2/3 complex (A) Representative maximum intensity projection over 14 seconds for cells expressing endogenous NeonGreen–ArpC5L, together with overexpressed Ruby–SPIN90 or Ruby–SPIN90-Nter. ArpC5L and Ruby–SPIN90, but not Ruby–SPIN90-Nter undergo rearward movement in the lamellipodium (highlighted with yellow arrows). The similar trajectory pattern observed in all the cells (20 for SPIN90-FL and 13 for SPIN90-Nter) across three independent replicates. (B) Representative live image (upper) of B16 cells with endogenously labelled NeonGreen-ArpC5L and overexpressing Ruby–SPIN90. Kymographs (lower), generated from the orange lines in the upper images, show that ArpC5L (left) and SPIN90 (right) exhibit directional movement, highlighted with blue arrows. Quantitative analysis (right panel) of the rearward flow of ArpC5L and SPIN90 respectively. Different colours indicate results from three independent replicates. A two-tailed unpaired t-test with Welsh’s correction is used to estimate the p-value. Scale bars = 5 µm

Techniques: Expressing, Generated, Two Tailed Test

Journal: bioRxiv

Article Title: SPIN90 modulates the architecture of lamellipodial actin in an ARPC5L dependent fashion

doi: 10.64898/2025.12.01.691495

Figure Lengend Snippet: SPIN90 enhances the recruitment of ArpC5L but not ArpC5 to the leading edge Representative images of live cells expressing endogenous NeonGreen–ArpC5L (A) or ArpC5-NeonGreen (B) after treatment with the indicated siRNAs. Allstar represents siRNA control. The graphs show quantification of the ArpC5L or ArpC5 signal intensity at the leading edge in the different conditions. Each point represents an individual cell, with different colours indicating 3 independent experimental replicates. For each repeat, 8-15 cells were imaged and quantified. The mean of each experiment is shown as a circle, and error bars are standard deviation. A two-tailed paired t-test was used to calculate the p-value. Scale bars = 5 µm

Techniques: Expressing, Control, Standard Deviation, Two Tailed Test

Journal: bioRxiv

Article Title: SPIN90 modulates the architecture of lamellipodial actin in an ARPC5L dependent fashion

doi: 10.64898/2025.12.01.691495

Figure Lengend Snippet: The organisation of actin filaments at the leading edge of B16 cells. (A) Schematic representation of ρ (rho) and ψ (psi) in the organization of the actin network. (B) Representative images of an Alexa-488 phalloidin stained B16 cell for each cell line as indicated. The coloured region in the lamellipodium is the result of polarimetry analysis within a 0.65 µm (10-pixel) region from the leading edge to determine the mean actin filament orientation in each pixel. The mean filament orientation per pixel is represented with a stick whose orientation corresponds to filament orientation (angle rho, ρ) and whose color depicts filament orientation with respect to the leading edge (angle rho c , ρ c ) within the 0–180° range according to the colour bar. The stick maps of a representative ROI (labelled with white rectangles) are zoomed in and shown. (C) The polar histogram shows the statistical distribution of actin filament angles (ρ c ) per pixel within the 0–90° range relative to the leading edge of all the cells, with 38 to 55 cells analysed per condition across three independent repeats. The average < ρ c > and standard deviation for each cell line are indicated. The colours correspond to the colour bar shown in panel A. (D) Violin plot showing the statistical distribution of actin filament angles (ρ c ) per pixel within the 0–90° range, as shown in panel B. A two-tailed Mann–Whitney test was used to calculate the p-value between individual cells under two conditions. The medians and interquartile ranges are shown as black lines, while the means and standard deviations are shown as blue dots with error bars. (E) The statistical results of the average lamellipodial actin filament angle < ρ c > relative to the leading edge within the 0–90° range in individual wildtype, ArpC5, ArpC5Lor SPIN90 knockout cells. Each point represents the mean angle of actin filaments relative to the leading edge in a single cell from three independent experiments, the latter shown in different colours. Mean ± SD for each experimental condition is indicated. A two-tailed Welch’s t-test is used to estimate the p-value between the means under two conditions. (F) The statistical results of the standard deviation (SD) of actin filament angles relative to the leading edge within the 0–90° range in individual wildtype, ArpC5, ArpC5L, or SPIN90 knockout cells. Each point represents the SD of actin filaments relative to the leading edge in a single cell from three independent experiments, the latter shown in different colours. Mean ± SD for each experimental condition is indicated. A two-tailed Mann Whitney test is used to estimate the p-value between individual cells under two conditions. (G) Representative images of Alexa-488 phalloidin stained B16 cell (right) overexpressing Ruby-SPIN90 (left). The zoomed-in image shows the mean actin filament orientation per pixel within the ROI (white rectangle) as in panel A. (H) The polar histogram shows the statistical distribution of actin filament angles (ρ c ) per pixel within the 0–90° range relative to the leading edge in all cells overexpressing either Ruby-SPIN90 (61 cells) or Ruby-SPIN90 Nter (59 cells), across three independent experimental repeats. The average < ρ c > and standard deviation for each experimental condition are indicated. The colours correspond to the colour bar shown in panel A.

Techniques: Staining, Standard Deviation, Two Tailed Test, MANN-WHITNEY, Knock-Out

Journal: bioRxiv

Article Title: SPIN90 modulates the architecture of lamellipodial actin in an ARPC5L dependent fashion

doi: 10.64898/2025.12.01.691495

Figure Lengend Snippet: Schematic summary (A) In migrating cells, SPIN90 recruits the ArpC5L-, but not the ArpC5-containing complex, to the lamellipodial leading edge . Meanwhile, both ArpC5L- and ArpC5-containing complexes generate branches at the lamellipodia . Thus, SPIN90 and Arp2/3 iso-complexes integrate into the lamellipodial actin network, contributing to the formation of a complex actin architecture that ensures efficient protrusion . (B) ArpC5 KO cells (left panel), the ArpC5L-containing complex participates in the formation of both linear and branched actin filaments. Consequently, the distribution of filament orientations in their lamellipodia is much fig than that of the wild type. In contrast, in ArpC5L KO cells (right panel), the ArpC5-containing complex generates only branched actin filaments, resulting in a narrower distribution of filament orientations.

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