Catch-slip bonds can be dispensable for motor force regulation during skeletal muscle contraction.
It is intriguing how multiple molecular motors can perform coordinated and synchronous functions, which is essential in various cellular processes. Recent studies on skeletal muscle might have shed light on this issue, where rather precise motor force regulation was partly attributed to the specific stochastic features of a single attached myosin motor. Though attached motors can randomly detach from actin filaments either through an adenosine triphosphate (ATP) hydrolysis cycle or through "catch-slip bond" breaking, their respective contribution in motor force regulation has not been clarified. Here, through simulating a mechanical model of sarcomere with a coupled Monte Carlo method and finite element method, we find that the stochastic features of an ATP hydrolysis cycle can be sufficient while those of catch-slip bonds can be dispensable for motor force regulation.
Department of Engineering Mechanics, Zhejiang University, Hangzhou, People's Republic of China.
Chenling
C
Dong
Department of Engineering Mechanics, Zhejiang University, Hangzhou, People's Republic of China.
Bin
B
Chen
D000199:Actins / Q000378:metabolism; D000255:Adenosine Triphosphate / Q000378:metabolism*; D003198:Computer Simulation; D004548:Elasticity; D020342:Finite Element Analysis; D006868:Hydrolysis; D008954:Models, Biological; D020409:Molecular Motor Proteins / Q000378:metabolism*; D009010:Monte Carlo Method; D009119:Muscle Contraction / Q000502:physiology*; D018482:Muscle, Skeletal / Q000502:physiology*; D013269:Stochastic Processes
D000199:Actins; D020409:Molecular Motor Proteins; D000255:Adenosine Triphosphate