The Vps39-like TRAP1 is an effector of Rab5 and likely the missing Vps3 subunit of human CORVET

Cellular Logistics
Jens LachmannChristian Ungermann

Abstract

Membrane fusion in the endocytic pathway is mediated by a protein machinery consistent of Rab GTPases, tethering factors and SNAREs. In yeast, the endosomal CORVET and lysosomal HOPS tethering complexes share 4 of their 6 subunits. The 2 additional subunits in each complex - Vps3 and Vps8 for CORVET, and the homologous Vps39 and Vps41 for HOPS - bind directly to Rab5 and Rab7, respectively. In humans, all subunits for HOPS have been described. However, human CORVET remains poorly characterized and a homolog of Vps3 is still missing. Here we characterize 2 previously identified Vps39 isoforms, hVps39-1/hVam6/TLP and hVps39-2/TRAP1, in yeast and HEK293 cells. None of them can compensate the loss of the endogenous yeast Vps39, though the specific interaction of hVps39-1 with the virus-specific LT protein was reproduced. Both human Vps39 proteins show a cytosolic localization in yeast and mammalian cells. However, hVps39-2/TRAP1 strongly co-localizes with co-expressed Rab5 and interacts directly with Rab5-GTP in vitro. We conclude that hVps39-2/TRAP1 is an endosomal protein and an effector of Rab5, suggesting a role of the protein as a subunit of the putative human CORVET complex.

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Citations

Jun 15, 2015·FEBS Letters·Anne KuhleeChristian Ungermann
Jul 28, 2016·Cell Discovery·Katie Powis, Claudio De Virgilio
Aug 27, 2015·Journal of Medical Genetics·Shimon EdvardsonOrly Elpeleg
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Jul 8, 2018·Journal of Cell Science·Naava Naslavsky, Steve Caplan
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May 28, 2021·FASEB Journal : Official Publication of the Federation of American Societies for Experimental Biology·Srinivasan RamakrishnanRoberto Docampo

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