Actinin-Associated LIM Protein: Identification of a Domain Interaction between PDZ and Spectrin-like Repeat Motifs

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...

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Bibliographic Details
Published in:The Journal of cell biology 1997-10, Vol.139 (2), p.507-515
Main Authors: Xia, Houhui, Winokur, Sara T., Kuo, Wen-Lin, Altherr, Michael R., Bredt, David S.
Format: Article
Language:English
Subjects:
Actinin - metabolism
Amino Acid Sequence
Amino acids
Animals
Base Sequence
Binding Sites
Cell Line
Cell lines
Cellular biology
Chromosome Mapping
Chromosomes
Chromosomes, Human, Pair 4
Complementary DNA
Genetic mutation
Genetic Variation
Humans
Karyotyping
LIM Domain Proteins
Messenger RNA
Microfilament Proteins - biosynthesis
Microfilament Proteins - chemistry
Microfilament Proteins - genetics
Molecular Sequence Data
Muscle, Skeletal - metabolism
Muscles
Muscular dystrophies
Muscular dystrophy
Neurons
Polymerase Chain Reaction
Proteins
Sequence Alignment
Sequence Homology, Amino Acid
Skeletal muscle
Spectrin - chemistry
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Summary: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 α-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 α-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 fascioscapulo-humeral muscular dystrophy.
ISSN:0021-9525
1540-8140
DOI:10.1083/jcb.139.2.507