K-29 linked ubiquitination of Arrdc4 regulates its function in extracellular vesicle biogenesis.

Extracellular Vesicles / metabolism Nedd4 Ubiquitin Protein Ligases / genetics Polyubiquitin / genetics Ubiquitin-Protein Ligases / genetics Ubiquitination
DMT1 Nedd4-2 Ubiquitin K-29 chains extracellular vesicles ubiquitination

Journal

Journal of extracellular vesicles
ISSN: 2001-3078
Titre abrégé: J Extracell Vesicles
Pays: United States
ID NLM: 101610479

Informations de publication

Date de publication:
02 2022
Historique:
revised: 14 12 2021
received: 18 04 2021
accepted: 02 01 2022
entrez: 2 2 2022
pubmed: 3 2 2022
medline: 5 4 2022
Statut: ppublish

Résumé

Extracellular vesicles (EVs) are important mediators of intercellular communication. However, EV biogenesis remains poorly understood. We previously defined a role for Arrdc4 (Arrestin domain containing protein 4), an adaptor for Nedd4 family ubiquitin ligases, in the biogenesis of EVs. Here we report that ubiquitination of Arrdc4 is critical for its role in EV secretion. We identified five potential ubiquitinated lysine residues in Arrdc4 using mass spectrometry. By analysing Arrdc4 lysine mutants we discovered that lysine 270 (K270) is critical for Arrdc4 function in EV biogenesis. Arrdc4

Identifiants

DOI: 10.1002/jev2.12188 PMID: 35106941 PMC: PMC8807422
pubmed: 35106941
doi: 10.1002/jev2.12188
pmc: PMC8807422
doi:

Substances chimiques

Polyubiquitin 120904-94-1
Nedd4 Ubiquitin Protein Ligases EC 2.3.2.26
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

e12188

Informations de copyright

© 2022 The Authors. Journal of Extracellular Vesicles published by Wiley Periodicals, LLC on behalf of the International Society for Extracellular Vesicles.

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Auteurs

Ammara Usman Farooq (AU)

Centre for Cancer Biology, University of South Australia, Adelaide, South Australia, Australia.

Kelly Gembus (K)

Centre for Cancer Biology, University of South Australia, Adelaide, South Australia, Australia.

Jarrod J Sandow (JJ)

Walter and Eliza Hall Institute, Parkville, Victoria, Australia.

Andrew Webb (A)

Walter and Eliza Hall Institute, Parkville, Victoria, Australia.

Suresh Mathivanan (S)

La Trobe Institute for Molecular Science, La Trobe University, Victoria, Australia.

Jantina A Manning (JA)

Centre for Cancer Biology, University of South Australia, Adelaide, South Australia, Australia.

Sonia S Shah (SS)

Centre for Cancer Biology, University of South Australia, Adelaide, South Australia, Australia.

Natalie J Foot (NJ)

Centre for Cancer Biology, University of South Australia, Adelaide, South Australia, Australia.

Sharad Kumar (S)

Centre for Cancer Biology, University of South Australia, Adelaide, South Australia, Australia.
ORCID: 0000-0001-7126-9814

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Classifications MeSH

questionsmedicales.fr › Cellules › Structures cellulaires › Espace extracellulaire › Vésicules extracellulaires › K-29 linked ubiquitination of Arrdc4 regulates...
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines membranaires › Protéines du transport vésiculaire › Complexes de tri endosomique requis pour le transport › Ubiquitine protéine ligases NEDD4 › K-29 linked ubiquitination of Arrdc4 regulates...
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Ubiquitines › Ubiquitine › Polyubiquitine › K-29 linked ubiquitination of Arrdc4 regulates...
questionsmedicales.fr › Enzymes et coenzymes › Enzymes › Ligases › Ubiquitin-protein ligase complexes › Ubiquitin-protein ligases › K-29 linked ubiquitination of Arrdc4 regulates...
questionsmedicales.fr › Phénomènes génétiques › Régulation de l'expression des gènes › Modification traductionnelle des protéines › Maturation post-traductionnelle des protéines › Ubiquitination › K-29 linked ubiquitination of Arrdc4 regulates...