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Molecular motors: structural adaptations to cellular functions

Nature volume 389, pages 561–567 (1997)Cite this article

Abstract

Molecular motors are protein machines whose directed movement along cytoskeletal filaments is driven by ATP hydrolysis. Eukaryotic cells contain motors that help to transport organelles to their correct cellular locations and to establish and alter cellular morphology during cell locomotion and division. The best-studied motors, myosin from skeletal muscle and conventional kinesin from brain, are remarkably similar in structure, yet have very different functions. These differences can be understood in terms of the ‘duty ratio’, the fraction of the time that a motor is attached to its filament. Differences in duty ratio can explain the diversity of structures, speeds and oligomerization states of members of the large kinesin, myosin and dynein families of motors.

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Figure 1: Structures of conventional kinesin and muscle myosin based on electron microscopy and sequence analysis.
Figure 2: The crossbridge cycle.
Figure 3: Structural and chemical models for the movement of a, kinesin, and b, myosin.
Figure 4: Ways in which myosin might increase its working stroke.

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Acknowledgements

This review was written while the author was a Guggenheim fellow on sabbatical leave in the Abteilung Molekulare Zellforschung, Max-Planck-Institut für Medicinische Forschung, Heidelberg. Original research was supported by the NIH and the Human Frontier Science Program. I thank many colleagues in Seattle and Heidelberg as well as M. Geeves, H. Gutfreund and M. Irving for critical comments on earlier drafts of the manuscript.

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Howard, J. Molecular motors: structural adaptations to cellular functions. Nature 389, 561–567 (1997). https://doi.org/10.1038/39247

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