Myosin-1c Interacts with Hair-Cell Receptors through Its Calmodulin-Binding IQ Domains

Janet L. Cyr, Rachel A. Dumont, Peter G. Gillespie

Research output: Contribution to journalArticlepeer-review

55 Scopus citations


Myosin-1c plays an essential role in adaptation of hair-cell mechanoelectrical transduction. To mediate adaptation, myosin-1c must interact directly or indirectly with other components of the transduction apparatus, including the mechanically gated transduction channel. As a first step toward identifying myosin-1c receptors, we used recombinant myosin-1c fragments to identify specific binding sites in hair cells and to biochemically characterize their interaction with myosin-1c. Myosin-1c fragments bound to tips of hair-cell stereocilia, the location of transduction and adaptation. Surprisingly, this interaction did not depend on the C-terminal tail of myosin-1c, proposed previously to be the receptor-binding site of the molecule. Instead, the interaction of myosin-1c with stereociliary receptors depended on its calmodulin-binding IQ domains. This interaction was blocked by calmodulin, which probably bound to a previously unoccupied IQ domain of myosin-1c. The calcium-sensitive binding of calmodulin to myosin-1c may therefore modulate the interaction of the adaptation motor with other components of the transduction apparatus.

Original languageEnglish (US)
Pages (from-to)2487-2495
Number of pages9
JournalJournal of Neuroscience
Issue number7
StatePublished - Apr 1 2002


  • Adaptation
  • Calmodulin
  • Hair bundle
  • Hair cell
  • IQ domain
  • Myo1c
  • Myosin-1c
  • Myosin-1β
  • Stereocilia
  • Transduction

ASJC Scopus subject areas

  • Neuroscience(all)


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