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  An actin-dependent mechanism for long-range vesicle transport.

Schuh, M. (2011). An actin-dependent mechanism for long-range vesicle transport. Nature Cell Biology, 13(12), 1431-1436. doi:10.1038/ncb2353.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002A-204B-A Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002A-2059-A
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 Creators:
Schuh, M.1, Author              
Affiliations:
1Department of Meiosis, MPI for Biophysical Chemistry, Max Planck Society, ou_2205654              

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 Abstract: Intracellular transport is vital for the function, survival and architecture of every eukaryotic cell. Long-range transport in animal cells is thought to depend exclusively on microtubule tracks. This study reveals an unexpected actin-dependent but microtubule-independent mechanism for long-range transport of vesicles. Vesicles organize their own actin tracks by recruiting the actin nucleation factors Spire1, Spire2 and Formin-2, which assemble an extensive actin network from the vesicles’ surfaces. The network connects the vesicles with one another and with the plasma membrane. Vesicles move directionally along these connections in a myosin-Vb-dependent manner to converge and to reach the cell surface. The overall outward-directed movement of the vesicle-actin network is driven by recruitment of vesicles to the plasma membrane in the periphery of the oocyte. Being organized in a dynamic vesicle-actin network allows vesicles to move in a local random manner and a global directed manner at the same time: they can reach any position in the cytoplasm, but also move directionally to the cell surface as a collective. Thus, collective movement within a network is a powerful and flexible mode of vesicle transport.

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Language(s): eng - English
 Dates: 2011-10-092011
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Identifiers: DOI: 10.1038/ncb2353
 Degree: -

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Title: Nature Cell Biology
Source Genre: Journal
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Pages: - Volume / Issue: 13 (12) Sequence Number: - Start / End Page: 1431 - 1436 Identifier: -