Unique features of myosin VI: a structural view

Abstract

Myosin VI is the only known molecular motor for the transportation of cargo vesicles from the plus end to the minus end of actin filaments. Thus, myosin VI possesses several unique features to distinguish it from other myosin family motors, such as the ability to move in a reverse direction, the unusual large walking step size, and the cargo-mediated dimerization. Recent structural studies of myosin VI have provided mechanistic insights into these unique features. On the basis of the resolved structures of myosin VI each domains (i.e., the structures of the N-terminal motor domain, the C-terminal cargo binding domain, and the region in the middle), the unique features of myosin VI will be reviewed here from a structural perspective. The structural studies of myosin VI definitely provide some answers about the unique features of myosin VI, but also raise significant questions on how myosin VI functions as a special motor both for directional cargo transport and for structural anchoring.

Keywords

molecular motor / myosin VI / cargo transport / cargo binding / walking step size

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Acknowledgements:

We would like to apologize for not being able to cite many original papers from colleagues due to space constraints. We thank Dr. Conan WANG for critical reading of the manuscript. W. F. is supported by the One Hundred Person Project and the Knowledge Innovation Program of the Chinese Academy of Sciences (KSCX2-YW-R-154).

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2014 Higher Education Press and Springer-Verlag Berlin Heidelberg