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The Journal of Neuroscience, April 1, 2002, 22(7):2487-2495
Myosin-1c Interacts with Hair-Cell Receptors through Its
Calmodulin-Binding IQ Domains
Janet L.
Cyr,
Rachel A.
Dumont, and
Peter G.
Gillespie
Oregon Hearing Research Center and Vollum Institute, Oregon Health
and Science University, Portland, Oregon 97201
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.
Key words:
Key words or phrases: adaptation; calmodulin; hair cell; hair
bundle; Myo1c; myosin-1c; myosin I ; IQ domain; stereocilia; transduction
Copyright © 2002 Society for Neuroscience 0270-6474/02/2272487-09$05.00/0
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