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Goliath family E3 ligases regulate the recycling endosome pathway via VAMP3 ubiquitylation
Umeå University, Faculty of Medicine, Department of Molecular Biology (Faculty of Medicine).
Umeå University, Faculty of Medicine, Department of Molecular Biology (Faculty of Medicine).
Umeå University, Faculty of Medicine, Department of Molecular Biology (Faculty of Medicine).
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2013 (English)In: EMBO Journal, ISSN 0261-4189, E-ISSN 1460-2075, Vol. 32, no 4, 524-537 p.Article in journal (Refereed) Published
Abstract [en]

Diverse cellular processes depend on endocytosis, intracellular vesicle trafficking, sorting and exocytosis, processes regulated post-transcriptionally by modifications such as phosphorylation and ubiquitylation. In addition to sorting to the lysosome, cargo is recycled to the plasma membrane via recycling endosomes. Here, we describe a role of the goliath gene family of protease-associated (PA) domain E3 ligases in regulating recycling endosome trafficking. The two Drosophila members of this family-Goliath and Godzilla(CG10277) - are located on endosomes, and both ectopic expression and loss-of-function lead to the accumulation of Rab5-positive giant endosomes. Furthermore, the human homologue RNF167 exhibits similar behaviour. We show that the soluble N-ethylmaleimide-sensitive fusion attachment protein receptor (SNARE) protein VAMP3 is a target of these ubiquitin ligases, and that recycling endosome trafficking is abrogated in response to their activity. Furthermore, mutation of the Godzilla ubiquitylation target lysines on VAMP3 abrogates the formation of enlarged endosomes induced by either Godzilla or RNF167. Thus, Goliath ubiquitin ligases play a novel role in regulating recycling endosome trafficking via ubiquitylation of the VAMP3 SNARE protein.

Place, publisher, year, edition, pages
Nature Publishing Group, 2013. Vol. 32, no 4, 524-537 p.
Keyword [en]
E3 ubiquitin ligase, goliath, RING domain, SNARE, VAMP3
National Category
Cell and Molecular Biology
Identifiers
URN: urn:nbn:se:umu:diva-68487DOI: 10.1038/emboj.2013.1ISI: 000316467200006OAI: oai:DiVA.org:umu-68487DiVA: diva2:618214
Available from: 2013-04-26 Created: 2013-04-22 Last updated: 2017-12-06Bibliographically approved

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Yamazaki, YasuoSchönherr, ChristinaDogru, MuratHallberg, BengtPalmer, Ruth H.
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