Myo1c is designed for the adaptation response in the inner ear.
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.
Batters
Christopher
C
Division of Physical Biochemistry, National Institutes for Medical Research, The Ridgeway, Mill Hill, London, UK.
Arthur
Christopher P
CP
Lin
Abel
A
Porter
Jessica
J
Geeves
Michael A
MA
Milligan
Ronald A
RA
Molloy
Justin E
JE
Coluccio
Lynne M
LM
D000220:Adaptation, Biological; D000244:Adenosine Diphosphate / Q000378:metabolism; D000818:Animals; D003051:Cochlea / Q000502:physiology*; D020285:Cryoelectron Microscopy; D006198:Hair Cells, Auditory / Q000166:cytology / Q000378:metabolism*; D040542:Mechanotransduction, Cellular / Q000502:physiology*; D051379:Mice; D008958:Models, Molecular; D009218:Myosins / Q000737:chemistry / Q000378:metabolism* / Q000648:ultrastructure; D051381:Rats; D013314:Stress, Mechanical
D000244:Adenosine Diphosphate; D009218:Myosins