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Dynamic exchange of myosin VI on endocytic structures.

The actin-based molecular motor myosin VI functions in the endocytic uptake pathway, both during the early stages of clathrin-mediated uptake and in later transport to/from early endosomes. This study uses fluorescence recovery after photobleaching (FRAP) to examine the turnover rate of myosin VI during endocytosis. The results demonstrate that myosin VI turns over dynamically on endocytic structures with a characteristic half-life common to both the large insert isoform of myosin VI on clathrin-coated structures and the no-insert isoform on early endosomes. This half-life is shared by the myosin VI-binding partner Dab2 and is identical for full-length myosin VI and the cargo-binding tail region. The 4-fold slower half-life of an artificially dimerized construct of myosin VI on clathrin-coated structures suggests that wild type myosin VI does not function as a stable dimer, but either as a monomer or in a monomer/dimer equilibrium. Taken together, these FRAP results offer insight into both the basic turnover dynamics and the monomer/dimer nature of myosin VI.

Pubmed ID: 22992744


  • Bond LM
  • Arden SD
  • Kendrick-Jones J
  • Buss F
  • Sellers JR


The Journal of biological chemistry

Publication Data

November 9, 2012

Associated Grants

  • Agency: Medical Research Council, Id: MC_U105184323
  • Agency: Intramural NIH HHS, Id:
  • Agency: Medical Research Council, Id:
  • Agency: Wellcome Trust, Id:

Mesh Terms

  • Animals
  • CHO Cells
  • Clathrin
  • Cricetinae
  • Dimerization
  • Endocytosis
  • Endosomes
  • Green Fluorescent Proteins
  • HeLa Cells
  • Humans
  • Models, Biological
  • Myosin Heavy Chains
  • Myosins
  • Photobleaching
  • Protein Isoforms
  • Two-Hybrid System Techniques