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PMID: 1425662 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Localization and identification of actin structures involved in the filamin-actin interaction.

European journal of biochemistry ·Vol. 209 ·No. 2 ·1992-10-15 ·Pages 555-62

Méjean C, Lebart MC, Boyer M, Roustan C, Benyamin Y

Abstract

The interface between gizzard filamin and skeletal muscle actin was located on the actin monomer. Conserved sequences 105-120 and 360-372, in the actin subdomain 1 near the myosin binding sites, were involved in this interaction. The corresponding peptides for these sequences were each found to bind filamin and compete in the actin-filamin interaction. When these two peptides were used together in the presence of filamin and filamentous actin, they dissociated sedimentable complexes formed by these two proteins.

MeSH Terms
Actins/chemistry,metabolism Amino Acid Sequence Animals Carrier Proteins/metabolism Chickens Contractile Proteins/isolation & purification,metabolism Electrophoresis, Polyacrylamide Gel Filamins Fluorescent Dyes Kinetics Microfilament Proteins/isolation & purification,metabolism Muscle, Smooth/metabolism Muscles/metabolism Naphthalenesulfonates Peptide Fragments/isolation & purification Protein Binding Rabbits Tropomyosin/metabolism
Chemicals
Actins Carrier Proteins Contractile Proteins Filamins Fluorescent Dyes Microfilament Proteins Naphthalenesulfonates Peptide Fragments Tropomyosin 1,5-I-AEDANS
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Méjean C
UPR 8402 Centre de Recherches de Biochimie Macromoléculaire (Centre National de la Recherche Scientifique), U 249, Montpellier, France.
Lebart M C
Boyer M
Roustan C
Benyamin Y
Article Info
Journal
European journal of biochemistry
Abbr.
Eur J Biochem
ISSN
0014-2956
DOI
10.1111/j.1432-1033.1992.tb17320.x
Published
1992-10-15
Pages
555-62
Language
English
Region
England
NLM ID
0107600
Subset
IM
External Links
PubMed source DOI: 10.1111/j.1432-1033.1992.tb17320.x
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