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Dev Cell. 2012 Jul 17;23(1):166-80. doi: 10.1016/j.devcel.2012.04.019. Epub 2012 Jun 14.

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

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  • 1Institut Jacques Monod, UMR 7592, CNRS, Université Paris Diderot, Sorbonne Paris Cité, Paris, France.


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.

Copyright © 2012 Elsevier Inc. All rights reserved.

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