| Literature DB >> 9763625 |
A S Khromov1, A V Somlyo, A P Somlyo.
Abstract
1. The effect of thiophosphorylation of the regulatory myosin light chain (MLC20) on rigor stiffness was determined in permeabilized rabbit bladder smooth muscle. 2. Rigor stiffness of alpha-toxin-permeabilized smooth muscle was significantly increased by thiophosphorylation of MLC20. This increase may have been due to partial shortening (melting) in the proximal rod region and/or stiffening of the regulatory domain of the myosin head. 3. We suggest that phosphorylation of MLC20, by increasing the stiffness of the S1 lever arm and/or S2 hinge regions of the myosin molecule, favours separation of the two phosphorylated heads and consequent deinhibition of motor domain activity.Entities:
Mesh:
Substances:
Year: 1998 PMID: 9763625 PMCID: PMC2231214 DOI: 10.1111/j.1469-7793.1998.345be.x
Source DB: PubMed Journal: J Physiol ISSN: 0022-3751 Impact factor: 5.182