Modification of small ubiquitin-related modifier 2 (SUMO2) by phosphoubiquitin in HEK293T cells.
HEK293T, phosphorylation, post-translational modification, Ser65
SUMO2, ubiquitin, unanchored polyubiquitin
Journal
Proteomics
ISSN: 1615-9861
Titre abrégé: Proteomics
Pays: Germany
ID NLM: 101092707
Informations de publication
Date de publication:
08 2021
08 2021
Historique:
revised:
21
05
2021
received:
05
09
2020
accepted:
25
05
2021
pubmed:
5
6
2021
medline:
26
10
2021
entrez:
4
6
2021
Statut:
ppublish
Résumé
Additional complexity in the post-translational modification of proteins by ubiquitin is achieved by ubiquitin phosphorylation, for example within PINK1-parkin mediated mitophagy. We performed a preliminary proteomic analysis to identify proteins differentially modified by ubiquitin in HEK293T, compared to phosphomimetic ubiquitin (Ser65Asp), and identified small ubiquitin-related modifier 2 (SUMO2) as a candidate. By transfecting SUMO2 and its C-terminal-GG deletion mutant, along with phosphomimetic ubiquitin, we confirm that ubiquitin modifies SUMO2, rather than vice versa. Further investigations revealed that transfected SUMO2 can also be conjugated by endogenous phospho-Ser65-(poly)ubiquitin in HEK293T cells, pointing to a previously unappreciated level of complexity in SUMO2 modification, and that unanchored (substrate-free) polyubiquitin chains may also be subject to phosphorylation.
Identifiants
pubmed: 34086420
doi: 10.1002/pmic.202000234
doi:
Substances chimiques
SUMO2 protein, human
0
Small Ubiquitin-Related Modifier Proteins
0
Ubiquitin
0
Polyubiquitin
120904-94-1
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
e2000234Informations de copyright
© 2021 The Authors. Proteomics published by Wiley-VCH GmbH.
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