Quantitative SUMO proteomics identifies PIAS1 substrates involved in cell migration and motility.
Cell Movement
/ physiology
Cell Proliferation
Cytoskeletal Proteins
/ metabolism
Gene Knockout Techniques
HEK293 Cells
HeLa Cells
Humans
Protein Inhibitors of Activated STAT
/ genetics
Protein Interaction Maps
Proteomics
SUMO-1 Protein
/ genetics
Sequence Analysis, Protein
Small Ubiquitin-Related Modifier Proteins
/ genetics
Sumoylation
Ubiquitin-Protein Ligases
/ metabolism
Vimentin
/ metabolism
Journal
Nature communications
ISSN: 2041-1723
Titre abrégé: Nat Commun
Pays: England
ID NLM: 101528555
Informations de publication
Date de publication:
11 02 2020
11 02 2020
Historique:
received:
04
12
2018
accepted:
07
01
2020
entrez:
13
2
2020
pubmed:
13
2
2020
medline:
24
4
2020
Statut:
epublish
Résumé
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.
Identifiants
pubmed: 32047143
doi: 10.1038/s41467-020-14581-w
pii: 10.1038/s41467-020-14581-w
pmc: PMC7012886
doi:
Substances chimiques
Cytoskeletal Proteins
0
PIAS1 protein, human
0
Protein Inhibitors of Activated STAT
0
SUMO-1 Protein
0
Small Ubiquitin-Related Modifier Proteins
0
Vimentin
0
Ubiquitin-Protein Ligases
EC 2.3.2.27
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
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