GSBS Student Publications


A one-headed class V myosin molecule develops multiple large (approximately 32-nm) steps successively

UMMS Affiliation

Graduate School of Biomedical Sciences; Department of Physiology



Document Type


Medical Subject Headings

Actins; Adenosine Triphosphate; Animals; Binding Sites; Chickens; Microfilaments; Models, Biological; *Movement; Myosin Type V; Protein Engineering; Protein Structure, Tertiary; Protein Transport; Rabbits; Xenopus laevis


Life Sciences | Medicine and Health Sciences


Class V myosin (myosin-V) was first found as a processive motor that moves along an actin filament with large ( approximately 36-nm) successive steps and plays an important role in cargo transport in cells. Subsequently, several other myosins have also been found to move processively. Because myosin-V has two heads with ATP- and actin-binding sites, the mechanism of successive movement has been generally explained based on the two-headed structure. However, the fundamental problem of whether the two-headed structure is essential for the successive movement has not been solved. Here, we measure motility of engineered myosin-V having only one head by optical trapping nanometry. The results show that a single one-headed myosin-V undergoes multiple successive large (approximately 32-nm) steps, suggesting that a novel mechanism is operating for successive myosin movement.

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Citation: Proc Natl Acad Sci U S A. 2004 Jun 29;101(26):9630-5. Epub 2004 Jun 18. Link to article on publisher's site

DOI of Published Version


Related Resources

Link to Article in PubMed

Journal Title

Proceedings of the National Academy of Sciences of the United States of America

PubMed ID