Robust processivity of myosin v under off-axis loads

Yusuke Oguchi, Sergey V. Mikhailenko, Takashi Ohki, Adrian O. Olivares, Enrique M. De La Cruz, Shiniichi Ishiwata

Research output: Contribution to journalArticle

19 Citations (Scopus)

Abstract

The dimeric motor myosin V transports organelles along actin filament tracks over long distances in cells. Myosin V is a smart 'walker' that is able to swiftly adjust to variable 'road conditions' to continue its processive movement across dense cellular environments. Coordination between the two heads via intramolecular load modulates biochemical kinetics and ensures highly efficient unidirectional motion. However, little is known about how load-induced regulation of the processive stepping occurs in vivo, where myosin V experiences significant off-axis loads applied in various directions. To reveal how myosin V remains processive in cells, we measured the effect of the off-axis loads, applied to individual actomyosin V bonds in a range of angles, on the coordination between the two heads and myosin V processive stepping. We found that myosin V remains highly processive under diagonal loads owing to asymmetrical ADP affinities and that the native 6IQ lever optimizes the subunit coordination, which indicates that myosin V is designed to be an intracellular transporter.

Original languageEnglish
Pages (from-to)300-305
Number of pages6
JournalNature Chemical Biology
Volume6
Issue number4
DOIs
Publication statusPublished - 2010 Apr

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology

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    Oguchi, Y., Mikhailenko, S. V., Ohki, T., Olivares, A. O., De La Cruz, E. M., & Ishiwata, S. (2010). Robust processivity of myosin v under off-axis loads. Nature Chemical Biology, 6(4), 300-305. https://doi.org/10.1038/nchembio.322