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 fascioscapulohumeral muscular dystrophy.
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20 October 1997
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October 20 1997
Actinin-associated LIM Protein: Identification of a Domain Interaction between PDZ and Spectrin-like Repeat Motifs
Houhui Xia,
Houhui Xia
Departments of *Physiology, ‡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
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Sara T. Winokur,
Sara T. Winokur
Departments of *Physiology, ‡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
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Wen-Lin Kuo,
Wen-Lin Kuo
Departments of *Physiology, ‡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
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Michael R. Altherr,
Michael R. Altherr
Departments of *Physiology, ‡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
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David S. Bredt
David S. Bredt
Departments of *Physiology, ‡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
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Houhui Xia
Departments of *Physiology, ‡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
Sara T. Winokur
Departments of *Physiology, ‡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
Wen-Lin Kuo
Departments of *Physiology, ‡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
Michael R. Altherr
Departments of *Physiology, ‡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
David S. Bredt
Departments of *Physiology, ‡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
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: [email protected]
Received:
May 06 1997
Revision Received:
July 22 1997
Online ISSN: 1540-8140
Print ISSN: 0021-9525
1997
J Cell Biol (1997) 139 (2): 507–515.
Article history
Received:
May 06 1997
Revision Received:
July 22 1997
Citation
Houhui Xia, Sara T. Winokur, Wen-Lin Kuo, Michael R. Altherr, David S. Bredt; Actinin-associated LIM Protein: Identification of a Domain Interaction between PDZ and Spectrin-like Repeat Motifs . J Cell Biol 20 October 1997; 139 (2): 507–515. doi: https://doi.org/10.1083/jcb.139.2.507
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