Coordinated recruitment of Spir actin nucleators and myosin V motors to Rab11 vesicle membranes.
- Resource Type
- Academic Journal
- Authors
- Pylypenko O; Institut Curie, PSL Research University, CNRS, UMR 144, F-75005, Paris, France.; Welz T; University Hospital Regensburg, Regensburg, Germany.; Tittel J; Max Planck Institute of Biochemistry, Martinsried, Germany.; Kollmar M; Max Planck Institute for Biophysical Chemistry, Göttingen, Germany.; Chardon F; Institut Curie, PSL Research University, CNRS, UMR 144, F-75005, Paris, France.; Malherbe G; Institut Curie, PSL Research University, CNRS, UMR 144, F-75005, Paris, France.; Weiss S; University Hospital Regensburg, Regensburg, Germany.; Michel CI; University Hospital Regensburg, Regensburg, Germany.; Samol-Wolf A; University Hospital Regensburg, Regensburg, Germany.; Grasskamp AT; University Hospital Regensburg, Regensburg, Germany.; Hume A; University of Nottingham, Nottingham, United Kingdom.; Goud B; Institut Curie, PSL Research University, CNRS, UMR 144, F-75005, Paris, France.; Baron B; Institut Pasteur, Biophysics of Macromolecules and their Interactions, Paris, France.; CNRS, UMR 3528, Paris, France.; England P; Institut Pasteur, Biophysics of Macromolecules and their Interactions, Paris, France.; CNRS, UMR 3528, Paris, France.; Titus MA; Department of Genetics, Cell Biology and Development, University of Minnesota, Minneapolis, United States.; Schwille P; Max Planck Institute of Biochemistry, Martinsried, Germany.; Weidemann T; Max Planck Institute of Biochemistry, Martinsried, Germany.; Houdusse A; Institut Curie, PSL Research University, CNRS, UMR 144, F-75005, Paris, France.; Kerkhoff E; University Hospital Regensburg, Regensburg, Germany.
- Source
- Publisher: eLife Sciences Publications, Ltd Country of Publication: England NLM ID: 101579614 Publication Model: Electronic Cited Medium: Internet ISSN: 2050-084X (Electronic) Linking ISSN: 2050084X NLM ISO Abbreviation: Elife Subsets: MEDLINE
- Subject
- Language
- English
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.
Competing Interests: The authors declare that no competing interests exist.