Full-length myosin VI dimerizes and moves processively along actin filaments upon monomer clustering

Hyokeun Park, Bhagavathi Ramamurthy, Mirko Travaglia, Dan Safer, Li Qiong Chen, Clara Franzini-Armstrong, Paul R. Selvin, H. Lee Sweeney

Research output: Contribution to journalArticle

Abstract

Myosin VI is a reverse direction actin-based motor capable of taking large steps (30-36 nm) when dimerized. However, all dimeric myosin VI molecules so far examined have included nonnative coiled-coil sequences, and reports on full-length myosin VI have failed to demonstrate the existence of dimers. Herein, we demonstrate that full-length myosin VI is capable of forming stable, processive dimers when monomers are clustered, which move up to 1-2 μm in ∼30 nm, hand-over-hand steps. Furthermore, we present data consistent with the monomers being prevented from dimerizing unless they are held in close proximity and that dimerization is somewhat inhibited by the cargo binding tail. A model thus emerges that cargo binding likely clusters and initiates dimerization of full-length myosin VI molecules. Although this mechanism has not been previously described for members of the myosin superfamily, it is somewhat analogous to the proposed mechanism of dimerization for the kinesin Unc104.

Original languageEnglish (US)
Pages (from-to)331-336
Number of pages6
JournalMolecular cell
Volume21
Issue number3
DOIs
StatePublished - Feb 3 2006

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology

Fingerprint Dive into the research topics of 'Full-length myosin VI dimerizes and moves processively along actin filaments upon monomer clustering'. Together they form a unique fingerprint.

  • Cite this

    Park, H., Ramamurthy, B., Travaglia, M., Safer, D., Chen, L. Q., Franzini-Armstrong, C., Selvin, P. R., & Sweeney, H. L. (2006). Full-length myosin VI dimerizes and moves processively along actin filaments upon monomer clustering. Molecular cell, 21(3), 331-336. https://doi.org/10.1016/j.molcel.2005.12.015