Article
- The EMBO Journal (2004) 23, 1433 - 1440
- doi:10.1038/sj.emboj.7600169
Published online: 11 March 2004
Subject Categories:
Myo1c is designed for the adaptation response in the inner ear
Christopher Batters1,a, Christopher P Arthur2,a, Abel Lin2,a, Jessica Porter3,a, Michael A Geeves4, Ronald A Milligan2, Justin E Molloy1 and Lynne M Coluccio3
- Division of Physical Biochemistry, National Institutes for Medical Research, The Ridgeway, Mill Hill, London, UK
- Center for Integrative Molecular Biosciences, The Scripps Research Institute, La Jolla, CA, USA
- Boston Biomedical Research Institute, Watertown, MA, USA
- Department of Biosciences, University of Kent, Canterbury, Kent, UK
Correspondence to:
Lynne M Coluccio, Boston Biomedical Research Institute, 64 Grove Street, Watertown, Boston, MA 2472-2829, USA. Tel.: +1 617 658 7784; Fax: +1 617 972 1761; E-mail: coluccio@bbri.org
aThese authors contributed equally to the work
Received 29 July 2003; Accepted 19 February 2004
Abstract
The molecular motor, Myo1c, a member of the myosin family, is widely expressed in vertebrate tissues. Its presence at strategic places in the stereocilia of the hair cells in the inner ear and studies using transgenic mice expressing a mutant Myo1c that can be selectively inhibited implicate it as the mediator of slow adaptation of mechanoelectrical transduction, which is required for balance. Here, we have studied the structural, mechanical and biochemical properties of Myo1c to gain an insight into how this molecular motor works. Our results support a model in which Myo1c possesses a strain-sensing ADP-release mechanism, which allows it to adapt to mechanical load.
Keywords:
- adaptation,
- molecular motor,
- Myo1c,
- myosin
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