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PMID: 2116421 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

An interaction between alpha-actinin and the beta 1 integrin subunit in vitro.

The Journal of cell biology ·Vol. 111 ·No. 2 ·1990-08-00 ·Pages 721-9

Otey CA, Pavalko FM, Burridge K

Abstract

A number of cytoskeletal-associated proteins that are concentrated in focal contacts, namely alpha-actinin, vinculin, talin, and integrin, have been shown to interact in vitro such that they suggest a potential link between actin filaments and the membrane. Because some of these interactions are of low affinity, we suspect the additional linkages also exist. Therefore, we have used a synthetic peptide corresponding to the cytoplasmic domain of beta 1 integrin and affinity chromatography to identify additional integrin-binding proteins. Here we report our finding of an interaction between the cytoplasmic domain of beta 1 integrin and the actin-binding protein alpha-actinin. Beta 1-integrin cytoplasmic domain peptide columns bound several proteins from Triton extracts of chicken embryo fibroblasts. One protein at approximately 100 kD was identified by immunoblot analysis as alpha-actinin. Solid phase binding assays indicated that alpha-actinin bound specifically and directly to the beta 1 peptide with relatively high affinity. Using purified heterodimeric chicken smooth muscle integrin (a beta 1 integrin) or the platelet integrin glycoprotein IIb/IIIa complex (a beta 3 integrin), binding of alpha-actinin was also observed in similar solid phase assays, albeit with a lower affinity than was seen using the beta 1 peptide. alpha-Actinin also bound specifically to phospholipid vesicles into which glycoprotein IIb/IIIa had been incorporated. These results lead us to suggest that this integrin-alpha-actinin linkage may contribute to the attachment of actin filaments to the membrane in certain locations.

MeSH Terms
Actinin/isolation & purification,metabolism Amino Acid Sequence Animals Cells, Cultured Chick Embryo Chromatography, Affinity Cytoskeletal Proteins/isolation & purification,metabolism Fibroblasts/metabolism Gizzard, Avian/metabolism Immunoblotting Integrins/metabolism Kinetics Macromolecular Substances Molecular Sequence Data Molecular Weight Muscle, Smooth/metabolism Peptides/chemical synthesis Phospholipids/metabolism Vinculin
Chemicals
Cytoskeletal Proteins Integrins Macromolecular Substances Peptides Phospholipids Actinin Vinculin
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Otey C A
Department of Cell Biology and Anatomy, University of North Carolina, Chapel Hill 27599.
Pavalko F M
Burridge K
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Article Info
Journal
The Journal of cell biology
Abbr.
J Cell Biol
ISSN
0021-9525
Published
1990-08-00
Pages
721-9
Language
English
Region
United States
NLM ID
0375356
PMCID
PMC2116186
Subset
IM
Grants
NCI NIH HHS · CA-08493 · United States
NIGMS NIH HHS · GM-29860 · United States
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