Linked Life Data

9334352

Source:http://linkedlifedata.com/resource/pubmed/id/9334352

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pubmed-article:9334352pubmed:abstractTextPDZ 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.lld:pubmed
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pubmed-article:9334352pubmed:authorpubmed-author:BreenD HDHlld:pubmed
pubmed-article:9334352pubmed:authorpubmed-author:AltherrM RMRlld:pubmed
pubmed-article:9334352pubmed:authorpubmed-author:XieLLlld:pubmed
pubmed-article:9334352pubmed:authorpubmed-author:LEEV TVTlld:pubmed
pubmed-article:9334352pubmed:authorpubmed-author:WinokurS TSTlld:pubmed
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