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Molecular motors: structural adaptations to cellular functions

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  • Joe Howard

    (University of Washington)

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.

Suggested Citation

  • Joe Howard, 1997. "Molecular motors: structural adaptations to cellular functions," Nature, Nature, vol. 389(6651), pages 561-567, October.
    • Handle: RePEc:nat:nature:v:389:y:1997:i:6651:d:10.1038_39247
    DOI: 10.1038/39247
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    Cited by:

    1. Rahimabadi, Arsalan & Benali, Habib, 2023. "Extended fractional-polynomial generalizations of diffusion and Fisher–KPP equations on directed networks," Chaos, Solitons & Fractals, Elsevier, vol. 174(C).
    2. Mallik, Roop & Gross, Steven P., 2006. "Molecular motors as cargo transporters in the cell—The good, the bad and the ugly," Physica A: Statistical Mechanics and its Applications, Elsevier, vol. 372(1), pages 65-69.
    3. Florian Berger & A J Hudspeth, 2017. "Chemomechanical regulation of myosin Ic cross-bridges: Deducing the elastic properties of an ensemble from single-molecule mechanisms," PLOS Computational Biology, Public Library of Science, vol. 13(5), pages 1-30, May.
    4. Lin, Lifeng & Wang, Huiqi & Ma, Hong, 2019. "Directed transport properties of double-headed molecular motors with balanced cargo," Physica A: Statistical Mechanics and its Applications, Elsevier, vol. 517(C), pages 270-279.

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