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Motor proteins

Another step ahead for myosin

Nature volume 398, pages 463–465 (1999)Cite this article

Eukaryotic cells contain many different protein motors, which use metabolic energy to transport cell components along polymer tracks such as actin filaments, microtubules or DNA. A single motor molecule moves along an isolated track in nanometre-scale steps corresponding to hydrolysis of single ATP molecules1,2,3,4. But two studies on myosin — the motor protein in muscle — by Veigel et al.5 ( page 530 of this issue) and Kitamura et al.6, show that each interaction with actin can include two or more sub-steps per ATP hydrolysed.

The head region of myosin, which embodies its motor function, contains a catalytic domain that binds actin and ATP, and an elongated carboxy-terminal domain containing a variable number of calmodulin-like light chains. The light-chain domain is thought to act as a lever arm in the motor mechanism7,8. It is often connected to its cargo (which may be a vesicle or filament) through a coiled-coil tail.

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Figure 1: Different ways in which a myosin S1 head might produce sub-steps as it moves along an actin filament.

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Authors and Affiliations

  1. Randall Institute, Kings College London, 26-29 Drury Lane, London, WC2B 5RL, UK

    Malcolm Irving

  2. Pennsylvania Muscle Institute, University of Pennsylvania, Philadelphia, 19104-6083, Pennsylvania , USA

    Yale E. Goldman

Authors
  1. Malcolm Irving
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  2. Yale E. Goldman
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Irving, M., Goldman, Y. Another step ahead for myosin . Nature 398, 463–465 (1999). https://doi.org/10.1038/18973

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