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Regulation of non‐muscle myosin structure and function
Author(s) -
Citi Sandra,
KendrickJones John
Publication year - 1987
Publication title -
bioessays
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.175
H-Index - 184
eISSN - 1521-1878
pISSN - 0265-9247
DOI - 10.1002/bies.950070404
Subject(s) - myosin , myosin light chain kinase , microbiology and biotechnology , phosphorylation , actin , immunoglobulin light chain , motility , vertebrate , biophysics , myosin head , cytoskeleton , meromyosin , biology , chemistry , biochemistry , cell , genetics , gene , antibody
In vertebrate and invertebrate nonmuscle myosins, light‐ and heavy‐chain phosphorylation regulate myosin assembly into filaments, and interaction with actin. Vertebrate non‐muscle myosins can exist in vitro in three main states, either ‘folded’ (assembly‐blocked) or ‘extended’ (assembly‐competent) monomers, and filaments. Light‐chain phosphorylation regulates the ‘dynamic equilibrium’ between these states. The ability of the myosin to undergo changes in conformation and state of assembly may be an important mechanism in regulating the organization of the cytoskeleton and cell motility.