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SHR Neuro Krebs Kardio Lipid Stoffw Microb

Cai, H; Yu, S; Menon, S; Cai, Y; Lazarova, D; Fu, C; Reinisch, K; Hay, JC; Ferro-Novick, S.
TRAPPI tethers COPII vesicles by binding the coat subunit Sec23.
Nature. 2007; 445(7130):941-944 Doi: 10.1038/nature05527
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Co-Autor*innen der Med Uni Graz
Hay Jesse
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Abstract:
The budding of endoplasmic reticulum (ER)-derived vesicles is dependent on the COPII coat complex. Coat assembly is initiated when Sar1-GTP recruits the cargo adaptor complex, Sec23/Sec24, by binding to its GTPase-activating protein (GAP) Sec23 (ref. 2). This leads to the capture of transmembrane cargo by Sec24 (refs 3, 4) before the coat is polymerized by the Sec13/Sec31 complex. The initial interaction of a vesicle with its target membrane is mediated by tethers. We report here that in yeast and mammalian cells the tethering complex TRAPPI (ref. 7) binds to the coat subunit Sec23. This event requires the Bet3 subunit. In vitro studies demonstrate that the interaction between Sec23 and Bet3 targets TRAPPI to COPII vesicles to mediate vesicle tethering. We propose that the binding of TRAPPI to Sec23 marks a coated vesicle for fusion with another COPII vesicle or the Golgi apparatus. An implication of these findings is that the intracellular destination of a transport vesicle may be determined in part by its coat and its associated cargo.
Find related publications in this database (using NLM MeSH Indexing)
Animals -
COP-Coated Vesicles - metabolism
Endoplasmic Reticulum - metabolism
GTPase-Activating Proteins -
Golgi Apparatus - metabolism
Membrane Fusion -
Membrane Proteins - metabolism
Multiprotein Complexes - metabolism
Protein Binding -
Saccharomyces cerevisiae - cytology
Saccharomyces cerevisiae - metabolism
Saccharomyces cerevisiae Proteins - metabolism
Vesicular Transport Proteins - metabolism
rab GTP-Binding Proteins - metabolism

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