Bro1 binds the Vps20 subunit of ESCRT-III and promotes ESCRT-III regulation by Doa4.


Journal

Traffic (Copenhagen, Denmark)
ISSN: 1600-0854
Titre abrégé: Traffic
Pays: England
ID NLM: 100939340

Informations de publication

Date de publication:
02 2022
Historique:
revised: 19 11 2021
received: 26 06 2021
accepted: 09 12 2021
pubmed: 16 12 2021
medline: 4 5 2022
entrez: 15 12 2021
Statut: ppublish

Résumé

The budding of intralumenal vesicles (ILVs) at endosomes requires membrane scission by the ESCRT-III complex. This step is negatively regulated in yeast by Doa4, the ubiquitin hydrolase that deubiquitinates transmembrane proteins sorted as cargoes into ILVs. Doa4 acts non-enzymatically to inhibit ESCRT-III membrane scission activity by directly binding the Snf7 subunit of ESCRT-III. This interaction inhibits the remodeling/disassembly of Snf7 polymers required for the ILV membrane scission reaction. Thus, Doa4 is thought to have a structural role that delays ILV budding while it also functions enzymatically to deubiquitinate ILV cargoes. In this study, we show that Doa4 binding to Snf7 in vivo is antagonized by another ESCRT-III subunit, Vps20. Doa4 is restricted from interacting with Snf7 in yeast expressing a mutant Vps20 allele that constitutively binds Doa4. This inhibitory effect of Vps20 is suppressed by overexpression of another ESCRT-III-associated protein, Bro1. We show that Bro1 binds directly to Vps20, suggesting that Bro1 has a central role in relieving the antagonistic relationship that Vps20 has toward Doa4.

Identifiants

pubmed: 34908216
doi: 10.1111/tra.12828
pmc: PMC8792227
mid: NIHMS1764596
doi:

Substances chimiques

Bro1 protein, S cerevisiae 0
Endosomal Sorting Complexes Required for Transport 0
Saccharomyces cerevisiae Proteins 0

Types de publication

Journal Article Research Support, N.I.H., Extramural

Langues

eng

Sous-ensembles de citation

IM

Pagination

109-119

Subventions

Organisme : NIGMS NIH HHS
ID : R01 GM111335
Pays : United States
Organisme : NIGMS NIH HHS
ID : T32 GM008759
Pays : United States
Organisme : NIGMS NIH HHS
ID : T32 GM142607
Pays : United States

Informations de copyright

© 2021 John Wiley & Sons A/S. Published by John Wiley & Sons Ltd.

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Auteurs

Dalton Buysse (D)

Department of Molecular Cellular and Developmental Biology, University of Colorado, Boulder, Colorado, USA.

Matt West (M)

Department of Molecular Cellular and Developmental Biology, University of Colorado, Boulder, Colorado, USA.

Mitchell Leih (M)

Department of Molecular Cellular and Developmental Biology, University of Colorado, Boulder, Colorado, USA.

Greg Odorizzi (G)

Department of Molecular Cellular and Developmental Biology, University of Colorado, Boulder, Colorado, USA.

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Classifications MeSH