Document Detail


alpha-actinin-2 is a new component of the dystrophin-glycoprotein complex.
MedLine Citation:
PMID:  10328815     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The human skeletal muscle yeast two-hybrid cDNA library was screened with the carboxyl-terminal region (the last 200 amino acids) of dystrophin. Two interacting clones were identified corresponding to alpha-actinin-2 and actin. Interactions between alpha-actinin, actin, and dystrophin were confirmed by the ligand-blotting technique, by colocalization of dystrophin and alpha-actinin-2 to the isolated skeletal muscle sarcolemmal vesicles and to the plasma membranes isolated from C2C12 myoblasts, and by indirect immunolocalization of dystrophin and alpha-actinin-2 in skeletal muscle cells. This is the first identification of a direct interaction between alpha-actinin, actin, and the carboxyl-terminal region of dystrophin. We propose that dystrophin forms lateral, multicontact association with actin and that binding of alpha-actinin-2 to the carboxyl-terminus of dystrophin is the communication link between the integrins and the dystrophin/dystrophin-glycoprotein complex.
Authors:
J E Hance; S Y Fu; S C Watkins; A H Beggs; M Michalak
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Archives of biochemistry and biophysics     Volume:  365     ISSN:  0003-9861     ISO Abbreviation:  Arch. Biochem. Biophys.     Publication Date:  1999 May 
Date Detail:
Created Date:  1999-06-11     Completed Date:  1999-06-11     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  0372430     Medline TA:  Arch Biochem Biophys     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  216-22     Citation Subset:  IM    
Copyright Information:
Copyright 1999 Academic Press.
Affiliation:
Department of Biochemistry, University of Alberta, Edmonton, Alberta, T6G 2H7, Canada.
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MeSH Terms
Descriptor/Qualifier:
Actinin / chemistry,  isolation & purification,  metabolism*
Actins / chemistry,  isolation & purification,  metabolism*
Cell Line
Cloning, Molecular
Dystrophin / chemistry,  isolation & purification,  metabolism*
Gene Library
Glycoproteins / chemistry,  isolation & purification,  metabolism*
Humans
Male
Models, Molecular
Muscle, Skeletal / metabolism
Protein Conformation
Recombinant Proteins / chemistry,  isolation & purification,  metabolism
Sarcolemma / chemistry,  metabolism
Chemical
Reg. No./Substance:
0/Actins; 0/Dystrophin; 0/Glycoproteins; 0/Recombinant Proteins; 11003-00-2/Actinin

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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