| Literature DB >> 15014434 |
Christopher Batters1, Christopher P Arthur, Abel Lin, Jessica Porter, Michael A Geeves, Ronald A Milligan, Justin E Molloy, Lynne M Coluccio.
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.Entities:
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Year: 2004 PMID: 15014434 PMCID: PMC391074 DOI: 10.1038/sj.emboj.7600169
Source DB: PubMed Journal: EMBO J ISSN: 0261-4189 Impact factor: 11.598