title: Muscle contraction and the elasticity-mediated crosstalk effect.
abstract: Cooperative action of molecular motors is essential for many cellular processes. One possible regulator of motor coordination is the elasticity-mediated crosstalk (EMC) coupling between myosin II motors whose origin is the tensile stress that they collectively generate in actin filaments. Here, we use a statistical mechanical analysis to investigate the influence of the EMC effect on the sarcomere -- the basic contractile unit of skeletal muscles. We demonstrate that the EMC effect leads to an increase in the attachment probability of motors located near the end of the sarcomere while simultaneously decreasing the attachment probability of the motors in the central part. Such a polarized attachment probability would impair the motors' ability to cooperate efficiently. Interestingly, this undesired phenomenon becomes significant only when the system size exceeds that of the sarcomere in skeletal muscles, which provides an explanation for the remarkable lack of sarcomere variability in vertebrates. Another phenomenon that we investigate is the recently observed increase in the duty ratio of the motors with the tension in muscle. We reveal that the celebrated Hill's equation for muscle contraction is very closely related to this observation.
authors.affiliation: Department of Biomedical Engineering, Ben Gurion University of the Negev, Be'er Sheva 84105, Israel.
authors.forename: Nadiv
authors.initials: N
authors.lastname: Dharan
authors.forename: Oded
authors.initials: O
authors.lastname: Farago
mesh_terms: D000818:Animals; D003198:Computer Simulation; D055119:Elastic Modulus / Q000502:physiology; D006801:Humans; D008954:Models, Biological; D015233:Models, Statistical; D020409:Molecular Motor Proteins / Q000502:physiology*; D009119:Muscle Contraction / Q000502:physiology*; D012518:Sarcomeres / Q000502:physiology*
chemical_list: D020409:Molecular Motor Proteins