5JCY

Spir2-GTBM bound to MyoVa-GTD

Summary for 5JCY

• Entry DOI: 10.2210/pdb5jcy/pdb
• Descriptor: Unconventional myosin-Va, Protein spire homolog 2 (3 entities in total)
• Functional Keywords: myosin, complex, spir actin nucleator, motor protein
• Biological source: Homo sapiens (Human); More
• Cellular location: Cytoplasm, cytoskeleton : Q8WWL2
• Total number of polymer chains: 2
• Total formula weight: 48539.19

Authors

Pylypenko, O.,Malherbes, G.,Welz, T.,Kerkhoff, E.,Houdusse, A. (deposition date: 2016-04-15, release date: 2016-09-28, Last modification date: 2024-01-10)

Primary citation

Pylypenko, O.,Welz, T.,Tittel, J.,Kollmar, M.,Chardon, F.,Malherbe, G.,Weiss, S.,Michel, C.I.,Samol-Wolf, A.,Grasskamp, A.T.,Hume, A.,Goud, B.,Baron, B.,England, P.,Titus, M.A.,Schwille, P.,Weidemann, T.,Houdusse, A.,Kerkhoff, E.
Coordinated recruitment of Spir actin nucleators and myosin V motors to Rab11 vesicle membranes.
Elife, 5:-, 2016

PubMed 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.

PubMed: 27623148
DOI: 10.7554/eLife.17523

Experimental method

X-RAY DIFFRACTION (1.8 Å)