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

Pylypenko, Olena; Welz, Tobias; Tittel, Janine; Kollmar, Martin; Chardon, Florian; Malherbe, Gilles; Weiss, Sabine; Michel, Carina Ida Luise; Samol-Wolf, Annette; Grasskamp, Andreas Till; Hume, Alistair; Goud, Bruno; Baron, Bruno; England, Patrick; Titus, Margaret A.; Schwille, Petra; Weidemann, Thomas; Houdusse, Anne; Kerkhoff, Eugen

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


Authors

Olena Pylypenko

Tobias Welz

Janine Tittel

Martin Kollmar

Florian Chardon

Gilles Malherbe

Sabine Weiss

Carina Ida Luise Michel

Annette Samol-Wolf

Andreas Till Grasskamp

Bruno Goud

Bruno Baron

Patrick England

Margaret A. Titus

Petra Schwille

Thomas Weidemann

Anne Houdusse

Eugen Kerkhoff



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.

Journal Article Type Article
Acceptance Date Aug 18, 2016
Online Publication Date Sep 13, 2016
Deposit Date Dec 19, 2017
Publicly Available Date Dec 19, 2017
Journal eLife
Electronic ISSN 2050-084X
Publisher eLife Sciences Publications
Peer Reviewed Peer Reviewed
Volume 5
Article Number e17523
DOI https://doi.org/10.7554/eLife.17523
Public URL https://nottingham-repository.worktribe.com/output/818147
Publisher URL https://elifesciences.org/articles/17523

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