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PMID: 9334352 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.

Actinin-associated LIM protein: identification of a domain interaction between PDZ and spectrin-like repeat motifs.

The Journal of cell biology ·Vol. 139 ·No. 2 ·1997-10-20 ·Pages 507-15

Xia H, Winokur ST, Kuo WL, Altherr MR, Bredt DS

Abstract

PDZ motifs are protein-protein interaction domains that often bind to COOH-terminal peptide sequences. The two PDZ proteins characterized in skeletal muscle, syntrophin and neuronal nitric oxide synthase, occur in the dystrophin complex, suggesting a role for PDZ proteins in muscular dystrophy. Here, we identify actinin-associated LIM protein (ALP), a novel protein in skeletal muscle that contains an NH2-terminal PDZ domain and a COOH-terminal LIM motif. ALP is expressed at high levels only in differentiated skeletal muscle, while an alternatively spliced form occurs at low levels in the heart. ALP is not a component of the dystrophin complex, but occurs in association with alpha-actinin-2 at the Z lines of myofibers. Biochemical and yeast two-hybrid analyses demonstrate that the PDZ domain of ALP binds to the spectrin-like motifs of alpha-actinin-2, defining a new mode for PDZ domain interactions. Fine genetic mapping studies demonstrate that ALP occurs on chromosome 4q35, near the heterochromatic locus that is mutated in fascioscapulohumeral muscular dystrophy.

MeSH Terms
Actinin/metabolism Amino Acid Sequence Animals Base Sequence Binding Sites Cell Line Chromosome Mapping Chromosomes, Human, Pair 4 Genetic Variation Humans Karyotyping LIM Domain Proteins Microfilament Proteins/biosynthesis,chemistry,genetics Molecular Sequence Data Muscle, Skeletal/metabolism Polymerase Chain Reaction Sequence Alignment Sequence Homology, Amino Acid Spectrin/chemistry
Chemicals
LIM Domain Proteins Microfilament Proteins PDLIM3 protein, human Pdlim3 protein, rat Actinin Spectrin
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Xia H
Department of Physiology, University of California at San Francisco, San Francisco, California 94143, USA.
Winokur S T
Kuo W L
Altherr M R
Bredt D S
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Article Info
Journal
The Journal of cell biology
Abbr.
J Cell Biol
ISSN
0021-9525
DOI
10.1083/jcb.139.2.507
Published
1997-10-20
Pages
507-15
Language
English
Region
United States
NLM ID
0375356
PMCID
PMC2139795
Subset
IM
External Links
PubMed source DOI: 10.1083/jcb.139.2.507 PMC Full Text View journal details
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