PulseExploreJournal ClubDebatesTrendingResearchersJournals
Instagram
HomeExploreJournal ClubTrending
Synapse
⌘+K
Synapse
January 1, 1982Cold Spring Harbor Symposia on Quantitative Biology28 citations

Regulation of Actin-Myosin Interaction by Reversible Phosphorylation of Myosin and Myosin Kinase

View Full Paper
RARobert AdelsteinMPM D PatoJSJ.R. Sellers

Key Result

Reversible phosphorylation of myosin and myosin kinase is the major regulatory mechanism controlling the interaction of actin and myosin in vertebrate smooth-muscle and non-muscle cells.

Structured PICO

P
Population
Vertebrate smooth-muscle and non-muscle cells

This review details the biochemical mechanisms of actin-myosin interaction regulation via phosphorylation in smooth and non-muscle cells.

Abstract

In this paper we deal with the regulation of contractile activity in vertebrate smooth-muscle and non-muscle cells. In particular, we focus on what is thought to be the major regulatory mechanism controlling the interaction of actin and myosin in these cells: the reversible phosphorylation of myosin and the enzyme myosin kinase (for review, see Adelstein and Eisenberg 1980; Hartshorne and Gorecka 1980).

Ask AI
Helpful
Bookmark
Share
View Full Paper

Cite This Study

Adelstein et al. (1982) conducted a review in Regulation of contractile activity in vertebrate smooth-muscle and non-muscle cells. Reversible phosphorylation of myosin and myosin kinase was evaluated on Interaction of actin and myosin. Reversible phosphorylation of myosin and myosin kinase is the major regulatory mechanism controlling the interaction of actin and myosin in vertebrate smooth-muscle and non-muscle cells.

synapsesocial.com/papers/6a309949912b1f0ec6bcaf02https://doi.org/10.1101/sqb.1982.046.01.086
Ask AI
Helpful
Bookmark
Share
View Full Paper