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  Coordinated recruitment of Spir actin nucleators and myosin V motors to Rab11 vesicle membranes.

Pylypenko, O., Welz, T., Tittel, J., Kollmar, M., Chardon, F., Malherbe, G., et al. (2016). Coordinated recruitment of Spir actin nucleators and myosin V motors to Rab11 vesicle membranes. eLife, 5: e17521. doi:10.7554/elife.17523.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002B-A2C8-3 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002B-A2CC-C
Genre: Journal Article

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 Creators:
Pylypenko, O., Author
Welz, T., Author
Tittel, J., Author
Kollmar, M.1, Author              
Chardon, F., Author
Malherbe, G., Author
Weiss, S., Author
Michel, C. I. L., Author
Samol-Wolf, A., Author
Grasskamp, A. T., Author
Hume, A., Author
Goud, B., Author
Baron, B., Author
England, P., Author
Titus, M. A., Author
Schwille, P., Author
Weidemann, T., Author
Houdusse, A., Author
Kerkhoff, E., Author
Affiliations:
1Research Group of Systems Biology of Motor Proteins, MPI for biophysical chemistry, Max Planck Society, ou_578570              

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 Abstract: There is growing evidence for a coupling of actin assembly and myosin motor activity in cells. However, mechanisms for recruitment of actin nucleators and motors on specific membrane compartments remain unclear. Here we report how Spir actin nucleators and myosin V motors coordinate their specific membrane recruitment. The myosin V globular tail domain (MyoV-GTD) interacts directly with an evolutionarily conserved Spir sequence motif. We determined crystal structures of MyoVa-GTD bound either to the Spir-2 motif or to Rab11 and show that a Spir-2:MyoVa:Rab11 complex can form. The ternary complex architecture explains how Rab11 vesicles support coordinated F-actin nucleation and myosin force generation for vesicle transport and tethering. New insights are also provided into how myosin activation can be coupled with the generation of actin tracks. Since MyoV binds several Rab GTPases, synchronized nucleator and motor targeting could provide a common mechanism to control force generation and motility in different cellular processes.

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Language(s): eng - English
 Dates: 2016-09-13
 Publication Status: Published online
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Identifiers: DOI: 10.7554/elife.17523
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Title: eLife
Source Genre: Journal
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Pages: 25 Volume / Issue: 5 Sequence Number: e17521 Start / End Page: - Identifier: -