Robust processivity of myosin v under off-axis loads

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

Research output: Contribution to journalArticle

18 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

Fingerprint

Myosin Type V
Myosins
Head
Actomyosin
Actin Cytoskeleton
Organelles
Adenosine Diphosphate

ASJC Scopus subject areas

  • Cell Biology
  • Molecular Biology

Cite this

Oguchi, Y., Mikhailenko, S., 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

Robust processivity of myosin v under off-axis loads. / Oguchi, Yusuke; Mikhailenko, Sergey; Ohki, Takashi; Olivares, Adrian O.; De La Cruz, Enrique M.; Ishiwata, Shiniichi.

In: Nature Chemical Biology, Vol. 6, No. 4, 04.2010, p. 300-305.

Research output: Contribution to journalArticle

Oguchi, Y, Mikhailenko, S, Ohki, T, Olivares, AO, De La Cruz, EM & Ishiwata, S 2010, 'Robust processivity of myosin v under off-axis loads', Nature Chemical Biology, vol. 6, no. 4, pp. 300-305. https://doi.org/10.1038/nchembio.322
Oguchi Y, Mikhailenko S, Ohki T, Olivares AO, De La Cruz EM, Ishiwata S. Robust processivity of myosin v under off-axis loads. Nature Chemical Biology. 2010 Apr;6(4):300-305. https://doi.org/10.1038/nchembio.322
Oguchi, Yusuke ; Mikhailenko, Sergey ; Ohki, Takashi ; Olivares, Adrian O. ; De La Cruz, Enrique M. ; Ishiwata, Shiniichi. / Robust processivity of myosin v under off-axis loads. In: Nature Chemical Biology. 2010 ; Vol. 6, No. 4. pp. 300-305.
@article{cdfef9da3a1e4756b3269a5710abad07,
title = "Robust processivity of myosin v under off-axis loads",
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.",
author = "Yusuke Oguchi and Sergey Mikhailenko and Takashi Ohki and Olivares, {Adrian O.} and {De La Cruz}, {Enrique M.} and Shiniichi Ishiwata",
year = "2010",
month = "4",
doi = "10.1038/nchembio.322",
language = "English",
volume = "6",
pages = "300--305",
journal = "Nature Chemical Biology",
issn = "1552-4450",
publisher = "Nature Publishing Group",
number = "4",

}

TY - JOUR

T1 - Robust processivity of myosin v under off-axis loads

AU - Oguchi, Yusuke

AU - Mikhailenko, Sergey

AU - Ohki, Takashi

AU - Olivares, Adrian O.

AU - De La Cruz, Enrique M.

AU - Ishiwata, Shiniichi

PY - 2010/4

Y1 - 2010/4

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=77949874333&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=77949874333&partnerID=8YFLogxK

U2 - 10.1038/nchembio.322

DO - 10.1038/nchembio.322

M3 - Article

C2 - 20228794

AN - SCOPUS:77949874333

VL - 6

SP - 300

EP - 305

JO - Nature Chemical Biology

JF - Nature Chemical Biology

SN - 1552-4450

IS - 4

ER -