Vps13 and Cdc31/centrin: Puzzling partners in membrane traffic

Author:

Myers Margaret D.1,Payne Gregory S.1ORCID

Affiliation:

1. Department of Biological Chemistry, David Geffen School of Medicine, University of California Los Angeles, Los Angeles, CA 90095

Abstract

Yeast Vps13 is a member of a conserved protein family that includes human homologues associated with neurodegenerative and developmental disorders. In this issue, De et al. (2017. J. Cell Biol. https://doi.org/10.1083/jcb.201606078) establish direct roles for Vps13 and its surprising binding partner, the calcium-binding centrin Cdc31, in trans-Golgi network (TGN) to endosome traffic and TGN homotypic fusion.

Funder

National Institutes of Health

Publisher

Rockefeller University Press

Subject

Cell Biology

Reference15 articles.

1. The Tlg SNARE complex is required for TGN homotypic fusion;Brickner;J. Cell Biol.,2001

2. Vps13p–Cdc31p complex is directly required for TGN late endosome transport and TGN homotypic fusion;De;J. Cell Biol.,2017

3. Using HHsearch to tackle proteins of unknown function: A pilot study with PH domains;Fidler;Traffic.,2016

4. Fine structure analysis of the yeast centrin, Cdc31p, identifies residues specific for cell morphology and spindle pole body duplication;Ivanovska;Genetics.,2001

5. Sfi1p has conserved centrin-binding sites and an essential function in budding yeast spindle pole body duplication;Kilmartin;J. Cell Biol.,2003

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