| First Author | Cyr JL | Year | 2002 |
| Journal | J Neurosci | Volume | 22 |
| Issue | 7 | Pages | 2487-95 |
| PubMed ID | 11923413 | Mgi Jnum | J:76010 |
| Mgi Id | MGI:2178207 | Doi | 10.1523/JNEUROSCI.22-07-02487.2002 |
| Citation | Cyr JL, et al. (2002) Myosin-1c interacts with hair-cell receptors through its calmodulin-binding IQ domains. J Neurosci 22(7):2487-95 |
| abstractText | 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. |
