compound mg132  (MedChemExpress)

Journal: bioRxiv

Article Title: PB-scope: Contrastive learning of dynamic processing body formation reveals undefined mechanisms of approved compounds

doi: 10.1101/2025.06.14.659731

Figure Lengend Snippet:

Article Snippet: The library of 278 FDA-approved kinase inhibitor compounds and small molecular compounds MG132 and thapsigargin were purchased from TargetMol ( ).

Techniques: Drug discovery

Journal: bioRxiv

Article Title: PB-scope: Contrastive learning of dynamic processing body formation reveals undefined mechanisms of approved compounds

doi: 10.1101/2025.06.14.659731

Figure Lengend Snippet: MG132 induces a continuous reduction in P-bodies over 8 hours, while thapsigargin causes a temporary decrease in their number from 1 to 3 hours, followed by recovery after 4 hours. These findings are consistent with previous findings – .

Article Snippet: The library of 278 FDA-approved kinase inhibitor compounds and small molecular compounds MG132 and thapsigargin were purchased from TargetMol ( ).

Techniques:

Journal: Nature Communications

Article Title: Targeting site-specific N-glycosylated B7H3 induces potent antitumor immunity

doi: 10.1038/s41467-025-58740-3

Figure Lengend Snippet: a Schematic diagram of human B7H3-NQ mutant constructs. WT B7H3 contains four pairs of Asn N-glycosylation sites at amino-acid positions 91 (N91) / 309 (N309), 104 (N104) / 322 (N322), 189 (N189) / 407 (N407) and 215 (N215) / 433 (N433) in the nearly exact tandem duplication of IgV-IgC domain. Potential asparagine N-glycosylation sites (N) were mutated to glutamine (Q). b HEK293T-B7H3KO cells were transiently re-expressed with the same amount of plasmids as indicated. Flow cytometry measuring B7H3 protein on the cell membrane in the indicated cell lines. Left, representative images of membrane B7H3. Right, median Fluorescence Intensity (MFI) of B7H3 ( n = 3 biological independent samples). c MDA-MB-231-B7H3KO cells and A549-B7H3KO were stably rescued with human B7H3-WT and B7H3-NQ mutant cDNA individually. Flow cytometry measuring B7H3 protein on the cell membrane in the indicated cells. d Schematic diagram of mouse B7H3-NQ mutant constructs. WT B7H3 contains four Asn N-glycosylation sites at amino-acid positions 91 (N91), 104 (N104), 189 (N189) and 215 (N215) in the single IgV-IgC domain. Potential asparagine N-glycosylation sites (N) were mutated to glutamine (Q). e 4T1-B7H3KO cells, B16-B7H3KO cells and E0771-B7H3KO cells were stably rescued with mouse B7H3-WT and B7H3-NQ mutant cDNA individually. Flow cytometry measuring B7H3 protein on the cell membrane in the indicated cell lines. f The indicated cell lines were treated with MG132 in the presence of CHX at indicated intervals. The intensity of B7H3 protein was quantified using ImageJ software. g The indicated cell lines were treated with MG132 for 6 h. Immunoprecipitation analysis of Flag-tagged B7H3 ubiquitination with the indicated antibodies. The p -value in ( b , f ) was determined by one-way ANOVA with Tukey’s multiple comparisons test. Error bars represent mean ± SD. Data in ( b – g ) are representative of three independent experiments.

Article Snippet: Compounds MG132 (Cat. S2619), NM-S873(Cat. S7285) and CB-5083(Cat. S8101) were obtained from Selleck Chemical.

Techniques: Mutagenesis, Construct, Glycoproteomics, Flow Cytometry, Membrane, Fluorescence, Stable Transfection, Software, Immunoprecipitation, Ubiquitin Proteomics

Journal: Nature Communications

Article Title: Targeting site-specific N-glycosylated B7H3 induces potent antitumor immunity

doi: 10.1038/s41467-025-58740-3

Figure Lengend Snippet: a IP-MS analysis showing candidates with increased binding to 8NQ or N91/104/309/322Q B7H3 compared to WT or N91/104/309/322Q B7H3. b The indicated cell lines were treated with MG132, NMS-873 (2 μM) or CB-5083 (5 μM) in the presence of CHX at indicated intervals. c The indicated cell lines were treated with NMS-873 or CB-5083. Immunoprecipitation analysis of Flag-tagged B7H3 ubiquitination with the indicated antibodies. d The indicated cell lines were treated with MG132 for 6 h. Flag-tagged B7H3 WT or its NQ mutants were pulled down by anti-Flag beads in the indicated cell lines, followed by western blotting to detect HRD1 and SEL1L. e MDA-MB-231-B7H3KO-N91/104/309/322Q cells were transiently transfected with HRD1 siRNA or SEL1L siRNA for 48 h. Then the cells were treated with CHX at indicated intervals. The intensity of B7H3 protein was quantified using ImageJ software. f MDA-MB-231-B7H3KO-N91/104/309/322Q cells expressing sgRNAs targeting HRD1 or SEL1L were treated with CHX at indicated intervals. The intensity of B7H3 protein was quantified using ImageJ software. g MDA-MB-231-B7H3KO-N91/104/309/322Q cells expressing sgRNAs targeting HRD1 or SEL1L were treated with MG132 for 6 h. Immunoprecipitation analysis of Flag-tagged B7H3 ubiquitination with the indicated antibodies. The p -value in ( e , f ) was determined by a two-tailed unpaired Student’s t -test. Error bars represent mean ± SD. Data in ( b – g ) are representative of three independent experiments.

Article Snippet: Compounds MG132 (Cat. S2619), NM-S873(Cat. S7285) and CB-5083(Cat. S8101) were obtained from Selleck Chemical.

Techniques: Protein-Protein interactions, Binding Assay, Immunoprecipitation, Ubiquitin Proteomics, Western Blot, Transfection, Software, Expressing, Two Tailed Test

Journal: eLife

Article Title: Impairment of lipid homeostasis causes lysosomal accumulation of endogenous protein aggregates through ESCRT disruption

doi: 10.7554/eLife.86194

Figure Lengend Snippet: ( A ) K562 cells treated with MG132 at 1 µM for 20 hr were stained with ProteoStat and imaged. Images with untreated and treated cells are shown here with the same grayscale. Inset: enlarged image of a single cell showing perinuclear ProteoStat punctates in MG132-treated cells. ( B ) Results of a reduced-scale batch retest to validate the effect of select sgRNAs from the genome-wide screen. Sequencing counts of each sgRNA in the FACS-sorted ProteoStat-high vs ProteoStat-low populations are shown. sgRNAs selected include ones that were enriched in the ProteoStat-high (red) and ProteoStat-low (blue) populations, or showed no enrichment (green) in the genome-wide screen, as well as non-targeting sgRNAs (gray) for normalization. ( C ) Effects of pharmacological inhibition of proteasome (MG132, 1 µM), lysosomal acidification (Bafilomycin A1, 6.25 µM), and chaperones (VER-155008, 50 µM; Ganetespib, 100 nM; 17-DMAG, 1 µM; n=1) on ProteoStat staining in K562 cells after the specified treatment durations. Figure 1—figure supplement 1—source data 1. CRISPRi ProteoStat batch retest sgRNA counts depicted in .

Article Snippet: chemical compound, drug , MG132 , EMD Millipore , 474790 , .

Techniques: Staining, Genome Wide, Sequencing, Inhibition

Journal: eLife

Article Title: Impairment of lipid homeostasis causes lysosomal accumulation of endogenous protein aggregates through ESCRT disruption

doi: 10.7554/eLife.86194

Figure Lengend Snippet: ( A ) ProteoStat validation: MG132-treated cells were stained, sorted into top and bottom quartiles (ProteoStat-high and ProteoStat-low, respectively), and imaged. ( B ) CRISPRi screen schematic: Untreated K562 cells were infected with sgRNA library, selected, stained, and sorted using gates that corrected for correlation between staining intensity and cell size. ( C ) A subset of GO Terms (Biological Process and Cellular Component) identified with GSEA on screen results. Positive Enrichment scores indicate an increased likelihood of genes in the GO Term to increase ProteoStat when knocked down. ( D ) Volcano plot highlighting major proteostasis pathways and select genes involved in lipid uptake and metabolism. Dotted line denotes where the product of |log 2 (fold-change)| and -log 10 (False discovery rate) is constant and equals to 1*-log 10 (0.05). Figure 1—source data 1. CRISPRi ProteoStat screen MAGeCK analysis combining inputs from two biological replicates; gene-level output. Depicted in .

Article Snippet: chemical compound, drug , MG132 , EMD Millipore , 474790 , .

Techniques: Biomarker Discovery, Staining, Infection

Journal: eLife

Article Title: Impairment of lipid homeostasis causes lysosomal accumulation of endogenous protein aggregates through ESCRT disruption

doi: 10.7554/eLife.86194

Figure Lengend Snippet: ( A & B ) Filipin III (A) and Proteostat (B) staining on K562 cells that were untreated or MBCD-treated to remove cholesterol. Same grayscale was used for each pair of images in the main panels, where an additional Filipin III image of the MBCD-treated cells was shown at enhanced-grayscale to expose the minimal filipin III staining on these cells. ( C ) Co-staining K562 cells (untreated or MG132-treated) against LAMP1 and with ProteoStat and Filipin III. ( D ) Biphasic GUVs with cholesterol-poor and cholesterol-rich phases were generated, which included TopFluor Cholesterol to label the cholesterol-rich phases. These GUVs were stained with ProteoStat at two concentrations – low (1:10000 diluted, as used in all other experiments, including FACS-based screen) and high (1:500 diluted). Unstained samples were included to assess background fluorescence in the ProteoStat channel.

Article Snippet: chemical compound, drug , MG132 , EMD Millipore , 474790 , .

Techniques: Staining, Generated, Fluorescence

Journal: eLife

Article Title: Impairment of lipid homeostasis causes lysosomal accumulation of endogenous protein aggregates through ESCRT disruption

doi: 10.7554/eLife.86194

Figure Lengend Snippet: ( A ) Effect on growth rates of various gene KDs. ( B ) Polyacrylamide gel with Silver Stain showing Lysosomal Insoluble fractions from cells treated with various concentrations of MG132 for 20 hr, followed by Lyso-IP and differential extraction. Figure 3—figure supplement 2—source data 1. PDF file containing original gel image for , indicating the treatment for each lane. Figure 3—figure supplement 2—source data 2. Original gel image for .

Article Snippet: chemical compound, drug , MG132 , EMD Millipore , 474790 , .

Techniques: Silver Staining, Extraction

Journal: eLife

Article Title: Impairment of lipid homeostasis causes lysosomal accumulation of endogenous protein aggregates through ESCRT disruption

doi: 10.7554/eLife.86194

Figure Lengend Snippet: ( A ) K562 cells stably expressing the pHLys sensor pHLARE were incubated with a pH buffer series in the presence of ionophores (nigericin and monensin) and analyzed with flow cytometry (n=3). ( B ) Effect of target gene KDs on LysoTracker vs LiperFluo phenotypes. R 2 value was obtained with a linear regression model (dotted blue line). ( C ) LysoTracker-Red staining in K562 CRISPRi cells carrying sgRNAs targeting various genes, which were either untreated or treated with the five antioxidant cocktail (5AO) for the duration of the gene KD. ( D ) SDS-PAGE in-gel fluorescence of lysates from cells treated with MG132 or Bortezomib for 1, 2, 4, or 20 hr before labeling with the Proteasome activity probe for 1 hour followed by lysis. Expected migration distances of different proteasome subunits are marked. ( E ) Effect of KDs of select genes in the mevalonate pathway on proteasome activity (n=1). ( F ) Transmission Electron Microscopy (TEM) images of K562 CRISPRi cells harvested 6 days after transduction of either non-targeting or PSAP-targeting sgRNAs. Figure 6—figure supplement 1—source data 1. PDF file containing original gel image for , indicating the treatment for each lane. Figure 6—figure supplement 1—source data 2. Original gel image for .

Article Snippet: chemical compound, drug , MG132 , EMD Millipore , 474790 , .

Techniques: Stable Transfection, Expressing, Incubation, Flow Cytometry, Staining, SDS Page, Fluorescence, Labeling, Activity Assay, Lysis, Migration, Transmission Assay, Electron Microscopy, Transduction

Journal: eLife

Article Title: Impairment of lipid homeostasis causes lysosomal accumulation of endogenous protein aggregates through ESCRT disruption

doi: 10.7554/eLife.86194

Figure Lengend Snippet:

Article Snippet: chemical compound, drug , MG132 , EMD Millipore , 474790 , .

Techniques: Membrane, Recombinant, Over Expression, Variant Assay, Construct, Sequencing, Modification, Clone Assay, Plasmid Preparation, Cholesterol Assay, Magnetic Beads, Software