ArticleNature communications2020
Quantitative SUMO proteomics identifies PIAS1 substrates involved in cell migration and motility.
Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.
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Who cites it
57 citing papers in PubMed, 76 citations in OpenAlex.
- Ubc9 Mediates SUMO2/3 Modification to Regulate Meiosis in Male Mice.Biomedicines · 2026Article
- A natural allele of TaSCE1-A1 confers drought resistance in wheat.Nature plants · 2026Article
- PIAS1-mediated GSK3β SUMOylation exacerbates tauopathy and cognitive deficits in Alzheimer's disease models.Molecular psychiatry · 2026Article
- A ZNF-nanobody fusion reveals SUMOylation-dependent changes in p53 protein localization.iScience · 2026Article
- A Landscape Analysis of Human SUMOylation.Molecular & cellular proteomics : MCP · 2026Article
- TRIM28 orchestrates SUMO-ubiquitin crosstalk to stabilize PPARG and drive bladder cancer progression.Cell death & disease · 2026Article
- Vimentin Intermediate Filaments: A Paradigm Shift From Static Structure to Dynamic Cytoplasmic Network.BioEssays : news and reviews in molecular, cellular and developmental biology · 2026Review
- Multi-omics analysis reveals PIAS family gene dysregulation as a driver of head and neck squamous cell carcinoma (HNSC) progression and therapeutic vulnerability.Discover oncology · 2025Article
- Hypoxia-Induced PRMT1 Lactylation Drives Vimentin Arginine Asymmetric Dimethylation in Tumor Metastasis.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Asprosin Aggravates Tubular Epithelial Cell Injury and Phenotypic Transformation via Mitochondrial Dynamics Disorder Mediated by Excessive Drp1 SUMOylation in Diabetic Nephropathy Mice.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- SUMOylation Regulates Neutrophil Phagocytosis and Migration.Pharmaceuticals (Basel, Switzerland) · 2025Article
- Structure and function of vimentin in the generation and secretion of extracellular vimentin in response to inflammation.Cell communication and signaling : CCS · 2025Review
- Dysregulation of protein SUMOylation networks in Huntington's disease R6/2 mouse striatum.Brain : a journal of neurology · 2025Article
- Epitope and Paratope Mapping of a SUMO-Remnant Antibody Using Cross-Linking Mass Spectrometry and Molecular Docking.Journal of proteome research · 2025Article
- The impact of dysregulation SUMOylation on prostate cancer.Journal of translational medicine · 2025Review
- SUMO2/3 conjugation of TDP-43 protects against aggregation.Science advances · 2025Article
- The role of SUMOylation in biomolecular condensate dynamics and protein localization.Cell insight · 2024Review
- Nuclear p62 condensates stabilize the promyelocytic leukemia nuclear bodies by sequestering their ubiquitin ligase RNF4.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- SENP1 mediates zinc-induced ZnT6 deSUMOylation at Lys-409 involved in the regulation of zinc metabolism in Golgi apparatus.Cellular and molecular life sciences : CMLS · 2024Article
- The role of ubiquitination in health and disease.MedComm · 2024Review
Corrections and comments
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The protein inhibitor of activated STAT1 (PIAS1) is an E3 SUMO ligase that plays important roles in various cellular pathways. Increasing evidence shows that PIAS1 is overexpressed in various human malignancies, including prostate and lung cancers. Here we used quantitative SUMO proteomics to identify potential substrates of PIAS1 in a system-wide manner. We identified 983 SUMO sites on 544 proteins, of which 62 proteins were assigned as putative PIAS1 substrates. In particular, vimentin (VIM), a type III intermediate filament protein involved in cytoskeleton organization and cell motility, was SUMOylated by PIAS1 at Lys-439 and Lys-445 residues. VIM SUMOylation was necessary for its dynamic disassembly and cells expressing a non-SUMOylatable VIM mutant showed a reduced level of migration. Our approach not only enables the identification of E3 SUMO ligase substrates but also yields valuable biological insights into the unsuspected role of PIAS1 and VIM SUMOylation on cell motility.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.