Crossref journal-article
Wiley
BioEssays (311)
Abstract

AbstractIn 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.

Bibliography

Citi, S., & Kendrick‐Jones, J. (1987). Regulation of non‐muscle myosin structure and function. BioEssays, 7(4), 155–159. Portico.

Dates
Type When
Created 20 years, 6 months ago (Feb. 25, 2005, 6:38 a.m.)
Deposited 1 year, 10 months ago (Oct. 21, 2023, 8:12 a.m.)
Indexed 5 months, 1 week ago (March 24, 2025, 2:45 a.m.)
Issued 37 years, 11 months ago (Oct. 1, 1987)
Published 37 years, 11 months ago (Oct. 1, 1987)
Published Online 20 years, 6 months ago (Feb. 5, 2005)
Published Print 37 years, 11 months ago (Oct. 1, 1987)
Funders 0

None

@article{Citi_1987, title={Regulation of non‐muscle myosin structure and function}, volume={7}, ISSN={1521-1878}, url={http://dx.doi.org/10.1002/bies.950070404}, DOI={10.1002/bies.950070404}, number={4}, journal={BioEssays}, publisher={Wiley}, author={Citi, Sandra and Kendrick‐Jones, John}, year={1987}, month=oct, pages={155–159} }