Protein phosphatase 6 dissociates the Beclin 1/Vps34 complex and inhibits autophagy.
Autophagy
Beclin 1
Protein-protein interaction
Serine/threonine protein phosphatase 6
Journal
Biochemical and biophysical research communications
ISSN: 1090-2104
Titre abrégé: Biochem Biophys Res Commun
Pays: United States
ID NLM: 0372516
Informations de publication
Date de publication:
07 05 2021
07 05 2021
Historique:
received:
11
02
2021
accepted:
26
02
2021
pubmed:
23
3
2021
medline:
29
6
2021
entrez:
22
3
2021
Statut:
ppublish
Résumé
Autophagy is an evolutionarily conserved intracellular degradation system and is regulated by various signaling pathways including the Beclin 1/Vacuolar protein sorting 34 (Vps34) complex. Protein phosphatase 6 (PP6) is an essential serine/threonine phosphatase that regulates various biological processes. Recently, we found that PP6 protein is degraded by p62-dependent selective autophagy. In this study, we show that PP6 conversely inhibits autophagy. PP6 associate with the C-terminal region of Beclin 1, which is close to the binding region of Vps34. The protein levels of PP6 affect Beclin 1/Vps34 complex formation and phosphatase activity of PP6 is not involved in this. We also show that chemically induced PP6/Beclin 1 association leads to Vps34 dissociation from Beclin 1. Overall, our data reveal a novel regulatory mechanism for autophagy by PP6.
Identifiants
pubmed: 33751937
pii: S0006-291X(21)00364-8
doi: 10.1016/j.bbrc.2021.02.136
pii:
doi:
Substances chimiques
Beclin-1
0
Multiprotein Complexes
0
Class III Phosphatidylinositol 3-Kinases
EC 2.7.1.137
Phosphoprotein Phosphatases
EC 3.1.3.16
protein phosphatase 6
EC 3.1.3.16
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
191-195Informations de copyright
Copyright © 2021 Elsevier Inc. All rights reserved.
Déclaration de conflit d'intérêts
Declaration of competing interest No potential conflict of interest was reported by the authors.