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PMID: 6430913 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. Review

Actin-membrane interaction in fibroblasts: what proteins are involved in this association?

The Journal of cell biology ·Vol. 99 ·No. 1 Pt 2 ·1984-07-00 ·Pages 95s-103s

Mangeat P, Burridge K

Abstract

In this review we discuss some of the proteins for which a role in linking actin to the fibroblast plasma membrane has been suggested. We focus on the family of proteins related to erythrocyte spectrin, proteins that have generally been viewed as having an organization and a function in actin-membrane attachment similar to those of erythrocyte spectrin. Experiments in which we precipitated the nonerythrocyte spectrin within living fibroblasts have led us to question this supposed similarity of organization and function of the nonerythrocyte and erythrocyte spectrins. Intracellular precipitation of fibroblast spectrin does not affect the integrity of the major actin-containing structures, the stress fiber microfilament bundles. Unexpectedly, however, we found that the precipitation of spectrin results in a condensation and altered distribution of the vimentin class of intermediate filaments in most cells examined. Although fibroblast spectrin may have a role in the attachment of some of the cortical, submembranous actin, it is surprising how little the intracellular immunoprecipitation of the spectrin affects the cells. Several proteins have been found concentrated at the ends of stress fibers, where the actin filaments terminate at focal contacts. Two of these proteins, alpha-actinin and fimbrin, have properties that suggest that they are not involved in the attachment of the ends of the bundles to the membrane but are more probably involved in the organization and cross-linking of the filaments within the bundles. On the other hand, vinculin and talin are two proteins that interact with each other and may form part of a chain of attachments between the ends of the microfilament bundles and the focal contact membrane. Their role in this attachment, however, has not been established and further work is needed to examine their interaction with actin and to identify any other components with which they may interact, particularly in the plasma membrane.

MeSH Terms
Actinin/metabolism Actins/metabolism Animals Carrier Proteins/metabolism Cell Membrane/metabolism Fibroblasts/cytology Fluorescent Antibody Technique Intermediate Filament Proteins/metabolism Membrane Proteins/metabolism Microfilament Proteins Muscle Proteins/metabolism Spectrin/metabolism Tissue Distribution Vimentin Vinculin
Chemicals
Actins Carrier Proteins Intermediate Filament Proteins Membrane Proteins Microfilament Proteins Muscle Proteins Vimentin fodrin Actinin Vinculin Spectrin
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Mangeat P
Burridge K
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73 references, click to expand
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Article Info
Journal
The Journal of cell biology
Abbr.
J Cell Biol
ISSN
0021-9525
DOI
10.1083/jcb.99.1.95s
Published
1984-07-00
Pages
95s-103s
Language
English
Region
United States
NLM ID
0375356
PMCID
PMC2275575
Subset
IM
Grants
NIGMS NIH HHS · GM 29860 · United States
External Links
PubMed source DOI: 10.1083/jcb.99.1.95s PMC Full Text View journal details
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