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PMID: 6129662 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

The structure of cortical cytoplasm.

Stossel TP

Abstract

Actin-rich cortical cytoplasm of phagocytic leucocytes forms pseudopodia and controls cell shape and movement by generating directional propulsive and contractile forces. Proteins purified from leucocytes form and deform an actin matrix. Actin-binding protein (ABP) cross-links actin filaments into a three-dimensional lattice with perpendicular branches. This structure, which can be visualized in the electron microscope, is consistent with physical properties of actin-ABP matrices. Gelsolin binds one end of actin filaments with high affinity in the presence of calcium; acumentin, another protein, constitutively binds the other end with low affinity. Together these proteins can control actin filament length and thereby regulate expansion (propulsion) or collapse of the actin network. The assembly state of the network also controls myosin-based contractile forces. A tug-of-war decides the direction of lattice movement, regions of lesser structure tending to move toward regions of greater structure.

MeSH Terms
Actins/metabolism Carrier Proteins/metabolism Cytoplasm/ultrastructure Cytoskeleton/ultrastructure Gelsolin Humans Leukocytes/ultrastructure Microfilament Proteins Microscopy, Electron Viscosity
Chemicals
Actins Carrier Proteins Gelsolin Microfilament Proteins brevin
Authors & Affiliations
1 authors, click to expand affiliations / ORCID
Stossel T P
Article Info
Journal
Philosophical transactions of the Royal Society of London. Series B, Biological sciences
Abbr.
Philos Trans R Soc Lond B Biol Sci
ISSN
0962-8436
Published
1982-11-04
Pages
275-89
Language
English
Region
England
NLM ID
7503623
Subset
IM
Grants
NCI NIH HHS · CA 06032 · United States
NHLBI NIH HHS · HL 19429 · United States
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