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

Houhui Xia, Sara T. Winokur, Wen-Lin Kuo, Michael R. Altherr and David S. Bredt
The Journal of Cell Biology
Vol. 139, No. 2 (Oct. 20, 1997), pp. 507-515
Stable URL: http://www.jstor.org/stable/1618266
Page Count: 9
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Actinin-Associated LIM Protein: Identification of a Domain Interaction between PDZ and Spectrin-like Repeat Motifs
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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 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.

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