Differential regulation of vertebrate myosins I and II

19Citations
Citations of this article
7Readers
Mendeley users who have this article in their library.

Abstract

Cell motility events require movement of the cytoskeleton. Actin-based movement is catalyzed by the mechanoenzyme myosin, which translocates toward the barbed end of actin filaments in an ATP-dependent fashion. There are two subclasses of myosin with different structures and functions: conventional filamentous myosin (myosin II) and monomeric myosin I. Vertebrate non-muscle myosins I and II function as similar actin motors in vitro, catalyzing virtually identical actin-activated MgATP hydrolysis and motility. The functional diversification of these two enzymes results from their differential regulation. Calcium and tropomyosin, which activate the MgATP hydrolysis and motility of vertebrate non-skeletal muscle myosin II proteins, inhibit vertebrate (brush border) myosin I. The activities and regulation of brush border myosin I provide insight into conserved and unique features of the myosin mechanoenzymes and suggest how the functions of myosin I and II are divided in vertebrate cells. Brush border myosin I as an enzyme also contributes to our understanding of the molecular mechanism of motility.

Cite

CITATION STYLE

APA

Collins, K., & Matsudaira, P. (1991). Differential regulation of vertebrate myosins I and II. In Journal of Cell Science (Vol. 98, pp. 11–16). https://doi.org/10.1242/jcs.1991.supplement_14.3

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free