Coordinated recruitment of Spir actin nucleators and myosin V motors to Rab11 vesicle membranes.
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.
Institut Curie, PSL Research University, CNRS, UMR 144, F-75005, Paris, France.
Olena
O
Pylypenko
University Hospital Regensburg, Regensburg, Germany.
Tobias
T
Welz
Max Planck Institute of Biochemistry, Martinsried, Germany.
Janine
J
Tittel
Max Planck Institute for Biophysical Chemistry, Göttingen, Germany.
Martin
M
Kollmar
Institut Curie, PSL Research University, CNRS, UMR 144, F-75005, Paris, France.
Florian
F
Chardon
Institut Curie, PSL Research University, CNRS, UMR 144, F-75005, Paris, France.
Gilles
G
Malherbe
University Hospital Regensburg, Regensburg, Germany.
Sabine
S
Weiss
University Hospital Regensburg, Regensburg, Germany.
Carina Ida Luise
CI
Michel
University Hospital Regensburg, Regensburg, Germany.
Annette
A
Samol-Wolf
University Hospital Regensburg, Regensburg, Germany.
Andreas Till
0000-0002-5895-6529
AT
Grasskamp
University of Nottingham, Nottingham, United Kingdom.
Alistair
A
Hume
Institut Curie, PSL Research University, CNRS, UMR 144, F-75005, Paris, France.
Bruno
B
Goud
Institut Pasteur, Biophysics of Macromolecules and their Interactions, Paris, France.|CNRS, UMR 3528, Paris, France.
Bruno
B
Baron
Institut Pasteur, Biophysics of Macromolecules and their Interactions, Paris, France.|CNRS, UMR 3528, Paris, France.
Patrick
P
England
Department of Genetics, Cell Biology and Development, University of Minnesota, Minneapolis, United States.
Margaret A
MA
Titus
Max Planck Institute of Biochemistry, Martinsried, Germany.
Petra
0000-0002-6106-4847
P
Schwille
Max Planck Institute of Biochemistry, Martinsried, Germany.
Thomas
T
Weidemann
Institut Curie, PSL Research University, CNRS, UMR 144, F-75005, Paris, France.
Anne
A
Houdusse
University Hospital Regensburg, Regensburg, Germany.
Eugen
0000-0002-3640-7916
E
Kerkhoff
D000818:Animals; D018360:Crystallography, X-Ray; D022162:Cytoplasmic Vesicles / Q000378:metabolism*; D008566:Membranes / Q000378:metabolism*; D051379:Mice; D008840:Microfilament Proteins / Q000737:chemistry / Q000378:metabolism*; D008958:Models, Molecular; D024701:Myosin Type V / Q000737:chemistry / Q000378:metabolism*; D011485:Protein Binding; D011487:Protein Conformation; D055503:Protein Multimerization; D020691:rab GTP-Binding Proteins / Q000737:chemistry / Q000378:metabolism*; D000099193:rab11 GTP-Binding Proteins
D008840:Microfilament Proteins; D024701:Myosin Type V; D020691:rab GTP-Binding Proteins; D000099193:rab11 GTP-Binding Proteins; C556674:Spir-2 protein, mouse
Rab11; Spire; actin motor proteins; actin nucleation; biophysics; cell biology; myosin V; none; structural biology; vesicle transport