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Molecular and Cellular Biology, March 2001, p. 1682-1687, Vol. 21, No. 5
0270-7306/01/$04.00+0   DOI: 10.1128/MCB.21.5.1682-1687.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Actinin-Associated LIM Protein-Deficient Mice Maintain Normal Development and Structure of Skeletal Muscle

Kiwon Jo,dagger Bart Rutten,Dagger Robert C. Bunn, and David S. Bredt*

Department of Physiology, University of California at San Francisco, San Francisco, California 94143

Received 4 August 2000/Returned for modification 28 September 2000/Accepted 7 December 2000

The actinin-associated LIM protein, ALP, is the prototype of a large family of proteins containing an N-terminal PDZ domain and a C-terminal LIM domain. These PDZ-LIM proteins are components of the muscle cytoskeleton and occur along the Z lines owing to interaction of the PDZ domain with the spectrin-like repeats of alpha -actinin. Because PDZ and LIM domains are typically found in proteins that mediate cellular signaling, PDZ-LIM proteins are suspected to participate in muscle development. Interestingly the ALP gene occurs at 4q35 near the heterochromatic region mutated in facioscapulohumeral muscular dystrophy, indicating a possible role for ALP in this disease. Here, we describe the generation and analysis of mice lacking the ALP gene. Surprisingly, the ALP knockout mice show no gross histological abnormalities and maintain sarcolemmal integrity as determined by serum pyruvate kinase assays. The absence of a dystrophic phenotype in these mice suggests that down-regulation of ALP does not participate in facioscapulohumeral muscular dystrophy. These data suggest that ALP does not participate in muscle development or that an alternative PDZ-LIM protein can compensate for the lack of ALP.

* Corresponding author. Mailing address: University of California at San Francisco School of Medicine, 513 Parnassus Ave., San Francisco, CA 94143-0444. Phone: (415) 476-6310. Fax: (415) 476-4929. E-mail: bredt{at}itsa.ucsf.edu.

dagger Present address: LG Chemical, Ltd., Life Science R&D, Taejon, Korea.

Dagger Present address: Faculty of Medicine, Maastricht University, Maastricht, The Netherlands.

Molecular and Cellular Biology, March 2001, p. 1682-1687, Vol. 21, No. 5
0270-7306/01/$04.00+0   DOI: 10.1128/MCB.21.5.1682-1687.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


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