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Goliath family E3 ligases regulate the recycling endosome pathway via VAMP3 ubiquitylation

Yamazaki, Yasuo, Schönherr, Christina, Varshney, Gaurav K, Dogru, Murat, Hallberg, Bengt, Palmer, Ruth H·2013·The EMBO Journal
DOI 10.1038/emboj.2013.1
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Abstract

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.

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Crossref · 10.1038/emboj.2013.1

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  • Ubiquitination events mediated by Drosophila Goliath family members regulate specific cellular events such as endocytosis and protein-protein interactions.

    “Ubiquitination events mediated by Drosophila Goliath family members have been shown to regulate specific cellular events such as endocytosis7,11 and protein-protein interactions12,13.”

    From RNF130 Regulates LDLR Availability and Plasma LDL Cholesterol Levels (2023) · cites this paper as [7]

  • Despite there being over 600 RING E3 ligases, only a small number, including RNF130, contain a bona fide transmembrane domain (TMD).

    “Despite there being over 600 RING E3 ligases6, only a small number, that includes RNF130, contain a bona fide transmembrane domain (TMD)7.”

    From RNF130 Regulates LDLR Availability and Plasma LDL Cholesterol Levels (2023) · cites this paper as [7]

  • This localization dictates target specificity and facilitates endocytic recycling of target proteins.

    “It was further shown that this localization dictates target specificity and facilitates endocytic recycling of target proteins.”

    From RNF130 Regulates LDLR Availability and Plasma LDL Cholesterol Levels (2023) · cites this paper as [7]

  • Previous studies of RNF167 and RNF13 have shown that these ligases are localized to both the plasma membrane and endosomes.

    “Previous studies of other PA-TM-RING ligase family members RNF167 and RNF13 have shown that these ligases are localized to both the plasma membrane and endosomes7.”

    From RNF130 Regulates LDLR Availability and Plasma LDL Cholesterol Levels (2023) · cites this paper as [7]

  • IDOL and GOLIATH are spatially separated within the cell, with IDOL localized to the plasma membrane and GOLIATH to the endosomal system.

    “It is noteworthy that IDOL and GOLIATH are spatially separated within the cell, with IDOL localized to the plasma membrane and GOLIATH to the endosomal system [65,81].”

    From The low-density lipoprotein receptor: Emerging post-transcriptional regulatory mechanisms (2025) · cites this paper as [81]

Citations

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Metadata

Authors
Yamazaki, Y., Schönherr, C., Varshney, G. K., Dogru, M., Hallberg, B., & Palmer, R. H.
Venue
The EMBO Journal
Publisher
Springer Science and Business Media LLC
Published
2013-01-25
Volume
32
Issue
4
Pages
524-537
ISSN
  • 0261-4189
  • 1460-2075
DOI
10.1038/emboj.2013.1
Cited by
55
References
6
Language
en
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