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ID 48821
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Author
Yamasaki, Akinori
Menon, Shekar
Yu, Sidney
Barrowman, Jemima
Meerloo, Timo
Oorschot, Viola
Klumperman, Judith
Ferro-Novick, Susan
Abstract
The GTPase Rab1 regulates endoplasmic reticulum-Golgi and early Golgi traffic. The guanine nucleotide exchange factor (GEF) or factors that activate Rab1 at these stages of the secretory pathway are currently unknown. Trs130p is a subunit of the yeast TRAPPII (transport protein particle II) complex, a multisubunit tethering complex that is a GEF for the Rab1 homologue Ypt1p. Here, we show that mammalian Trs130 (mTrs130) is a component of an analogous TRAPP complex in mammalian cells, and we describe for the first time the role that this complex plays in membrane traffic. mTRAPPII is enriched on COPI (Coat Protein I)-coated vesicles and buds, but not Golgi cisternae, and it specifically activates Rab1. In addition, we find that mTRAPPII binds to γ1COP, a COPI coat adaptor subunit. The depletion of mTrs130 by short hairpin RNA leads to an increase of vesicles in the vicinity of the Golgi and the accumulation of cargo in an early Golgi compartment. We propose that mTRAPPII is a Rab1 GEF that tethers COPI-coated vesicles to early Golgi membranes.
Published Date
2009-10-01
Publication Title
Molecular Biology of the Cell
Volume
volume20
Issue
issue19
Publisher
The American Society for Cell Biology
Start Page
4205
End Page
4215
ISSN
1059-1524
NCID
AA12024500
Content Type
Journal Article
Project
Research Core for Interdisciplinary Sciences
Official Url
http://www.molbiolcell.org/content/20/19/4205.full
language
英語
Copyright Holders
© 2009 by The American Society for Cell Biology
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publisher
Refereed
True
DOI
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