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A molecular network for the transport of the TI-VAMP/VAMP7 vesicles from cell center to periphery.

Authors: Burgo, A  Proux-Gillardeaux, V  Sotirakis, E  Bun, P  Casano, A  Verraes, A  Liem, RK  Formstecher, E  Coppey-Moisan, M  Galli, T 
Citation: Burgo A, etal., Dev Cell. 2012 Jul 17;23(1):166-80. doi: 10.1016/j.devcel.2012.04.019. Epub 2012 Jun 14.
Pubmed: (View Article at PubMed) PMID:22705394
DOI: Full-text: DOI:10.1016/j.devcel.2012.04.019

The compartmental organization of eukaryotic cells is maintained dynamically by vesicular trafficking. SNARE proteins play a crucial role in intracellular membrane fusion and need to be targeted to their proper donor or acceptor membrane. The molecular mechanisms that allow for the secretory vesicles carrying the v-SNARE TI-VAMP/VAMP7 to leave the cell center, load onto microtubules, and reach the periphery to mediate exocytosis are largely unknown. Here, we show that the TI-VAMP/VAMP7 partner Varp, a Rab21 guanine nucleotide exchange factor, interacts with GolginA4 and the kinesin 1 Kif5A. Activated Rab21-GTP in turn binds to MACF1, an actin and microtubule regulator, which is itself a partner of GolginA4. These components are required for directed movement of TI-VAMP/VAMP7 vesicles from the cell center to the cell periphery. The molecular mechanisms uncovered here suggest an integrated view of the transport of vesicles carrying a specific v-SNARE toward the cell surface.


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CRRD Object Information
CRRD ID: 10047362
Created: 2015-07-11
Species: All species
Last Modified: 2015-07-11
Status: ACTIVE


RGD is funded by grant HL64541 from the National Heart, Lung, and Blood Institute on behalf of the NIH.