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© The Rockefeller University Press, 0021-9525/1997//507 $5.00
The Journal of Cell Biology, Volume 139, Number 2, , 1997 507-515

Article

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



Houhui Xia*,{ddagger}, Sara T. Winokur||, Wen-Lin Kuo§, Michael R. Altherr||, and David S. Bredt*

Departments of * Physiology, {ddagger} 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

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.

Abbreviations used in this paper: ALP, actinin-associated LIM protein; EST, expressed sequence tag; FISH, fluorescence in situ hybridization; FSHD, fascioscapulohumoral muscular dystrophy; GST, glutathione S-transferase; INAD, inactivation no afterpotential D; nNOS, neuronal nitric oxide synthase; ORF, open reading frame; RT-PCR, reverse transcription; ZO, zona occludens.

Address all correspondence to David S. Bredt, University of California at San Francisco School of Medicine, 513 Parnassus Avenue, San Francisco, CA 94143-0444. Tel.: (415) 476-6310; Fax: (415) 476-4929; E-mail: bredt{at}itsa.ucsf.edu


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