GSBS Student Publications


Class VI myosin moves processively along actin filaments backward with large steps

UMMS Affiliation

Graduate School of Biomedical Sciences; Department of Physiology



Document Type


Medical Subject Headings

Actins; Adenosine Triphosphatases; Adenosine Triphosphate; Animals; Cell Line; DNA, Complementary; Green Fluorescent Proteins; Insects; Luminescent Proteins; Microscopy, Electron; Models, Biological; Muscle, Skeletal; Myosin Heavy Chains; Myosin Type V; Protein Binding; Rabbits; Recombinant Fusion Proteins; Recombinant Proteins; Time Factors; Xenopus


Life Sciences | Medicine and Health Sciences


Among a superfamily of myosin, class VI myosin moves actin filaments backwards. Here we show that myosin VI moves processively on actin filaments backwards with large ( approximately 36 nm) steps, nevertheless it has an extremely short neck domain. Myosin V also moves processively with large ( approximately 36 nm) steps and it is believed that myosin V strides along the actin helical repeat with its elongated neck domain that is critical for its processive movement with large steps. Myosin VI having a short neck cannot take this scenario. We found by electron microscopy that myosin VI cooperatively binds to an actin filament at approximately 36 nm intervals in the presence of ATP, raising a hypothesis that the binding of myosin VI evokes "hot spots" on actin filaments that attract myosin heads. Myosin VI may step on these "hot spots" on actin filaments in every helical pitch, thus producing processive movement with 36 nm steps.

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Citation: Biochem Biophys Res Commun. 2002 Jan 11;290(1):311-7. Link to article on publisher's site

DOI of Published Version


Related Resources

Link to article in PubMed

Journal Title

Biochemical and biophysical research communications

PubMed ID