Exploration of nuclear body-enhanced sumoylation reveals that PML represses 2-cell features of embryonic stem cells.
Journal
Nature communications
ISSN: 2041-1723
Titre abrégé: Nat Commun
Pays: England
ID NLM: 101528555
Informations de publication
Date de publication:
29 09 2022
29 09 2022
Historique:
received:
06
03
2021
accepted:
05
09
2022
entrez:
29
9
2022
pubmed:
30
9
2022
medline:
4
10
2022
Statut:
epublish
Résumé
Membrane-less organelles are condensates formed by phase separation whose functions often remain enigmatic. Upon oxidative stress, PML scaffolds Nuclear Bodies (NBs) to regulate senescence or metabolic adaptation. PML NBs recruit many partner proteins, but the actual biochemical mechanism underlying their pleiotropic functions remains elusive. Similarly, PML role in embryonic stem cell (ESC) and retro-element biology is unsettled. Here we demonstrate that PML is essential for oxidative stress-driven partner SUMO2/3 conjugation in mouse ESCs (mESCs) or leukemia, a process often followed by their poly-ubiquitination and degradation. Functionally, PML is required for stress responses in mESCs. Differential proteomics unravel the KAP1 complex as a PML NB-dependent SUMO2-target in arsenic-treated APL mice or mESCs. PML-driven KAP1 sumoylation enables activation of this key epigenetic repressor implicated in retro-element silencing. Accordingly, Pml
Identifiants
pubmed: 36175410
doi: 10.1038/s41467-022-33147-6
pii: 10.1038/s41467-022-33147-6
pmc: PMC9522831
doi:
Substances chimiques
DNA Transposable Elements
0
Dppa2 protein, mouse
0
Transcription Factors
0
Arsenic
N712M78A8G
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
5726Commentaires et corrections
Type : ErratumIn
Informations de copyright
© 2022. The Author(s).
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