hVps41 is expressed in multiple isoforms and can associate with vesicles through a RING-H2 finger motif

Diane McVey Ward, Derek Radisky, Matthew A. Scullion, Marie S. Tuttle, Michael Vaughn, Jerry Kaplan

Research output: Contribution to journalArticle

21 Scopus citations

Abstract

Vps41p, the protein encoded by the yeast gene VPS41, has been shown to mediate formation of AP-3 transport vesicles from the Golgi apparatus and to facilitate the docking and fusion of lysosomal vesicles. Although both of these activities involve transient association with membrane structures, the mechanisms that mediate those interactions have not been determined. Orthologues of VPS41 have been identified in humans, Drosophila, tomato, and Arabidopsis; the degree of sequence similarity among these genes suggests a highly conserved function. Here we provide evidence that hVps41, the human homologue of Vps41p, is expressed in two isoforms that differ in that one contains a C-terminal RING-H2 sequence motif. Transient expression analysis suggests that this RING-H2 domain is responsible for membrane association. This observation was further supported by the cytosolic localization of site-specific mutants. A truncated construct containing only the hVps41 RING-H2 domain was found to associate with a class of intracellular vesicles that originated from the Golgi and showed partial coincidence with the δ subunit of the adaptor protein complex-3. Together with information from the homologous yeast system, these results suggest that hVps41 may also be involved in the formation and fusion of transport vesicles from the Golgi.

Original languageEnglish (US)
Pages (from-to)126-134
Number of pages9
JournalExperimental Cell Research
Volume267
Issue number1
DOIs
StatePublished - Jul 1 2001

Keywords

  • AP-3
  • Protein sorting
  • RING-H2
  • Vps41

ASJC Scopus subject areas

  • Cell Biology

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