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Departments of * Physiology, 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 Pharmaceutical Chemistry, and § Molecular Cytometry, University of California at San Francisco,
San Francisco, California 94143; and Department of Biological Chemistry, University of California at Irvine, Irvine, California
92697
-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 -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.
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