Journal
EMBO JOURNAL
Volume 23, Issue 7, Pages 1433-1440Publisher
WILEY
DOI: 10.1038/sj.emboj.7600169
Keywords
adaptation; molecular motor; Myo1c; myosin
Categories
Funding
- Medical Research Council [MC_U117570592] Funding Source: Medline
- NCRR NIH HHS [RR17573, P41 RR017573] Funding Source: Medline
- NIGMS NIH HHS [GM068080, R01 GM061939, GM39155, GM61939, R01 GM068080] Funding Source: Medline
- Engineering and Physical Sciences Research Council [GR/R45659/01] Funding Source: researchfish
- Medical Research Council [MC_U117570592] Funding Source: researchfish
- MRC [MC_U117570592] Funding Source: UKRI
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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.
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