Adamek, N. and Coluccio, L.M. and Geeves, M.A. (2008) Calcium sensitivity of the cross-bridge cycle of Myo1c, the adaptation motor in the inner ear. Proceedings of the National Academy of Sciences of the United States of America. , 105 (15). pp. 5710-5715. ISSN 0027-8424.
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The class I myosin Myo1c is a mediator of adaptation of mechanoelectrical transduction in the stereocilia of the inner ear. Adaptation, which is strongly affected by Ca2+, permits hair cells under prolonged stimuli to remain sensitive to new stimuli. Using a Myo1c fragment (motor domain and one IQ domain with associated calmodulin), with biochemical and kinetic properties similar to those of the native molecule, we have performed a thorough analysis of the biochemical cross-bridge cycle. We show that, although the steady-state ATPase activity shows little calcium sensitivity, individual molecular events of the cross-bridge cycle are calcium-sensitive. Of significance is a 7-fold inhibition of the ATP hydrolysis step and a 10-fold acceleration of ADP release in calcium. These changes result in an acceleration of detachment of the cross-bridge and a lengthening of the lifetime of the detached M-ATP state. These data support a model in which slipping adaptation, which reduces tip-link tension and allows the transduction channels to close after an excitatory stimulus, is mediated by Myo1c and modulated by the calcium transient.
|Additional information:||070021/United Kingdom Wellcome Trust DC008793/DC/United States NIDCD GM68080/GM/United States NIGMS Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't United States|
|Uncontrolled keywords:||molecular motor; myosin|
|Divisions:||Faculties > Science Technology and Medical Studies > School of Biosciences > Protein Science Group|
|Depositing User:||Jane Griffiths|
|Date Deposited:||18 Apr 2009 10:14|
|Last Modified:||13 May 2009 09:31|
|Resource URI:||http://kar.kent.ac.uk/id/eprint/14689 (The current URI for this page, for reference purposes)|
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