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Molecular and Cellular Biology, January 2007, p. 244-252, Vol. 27, No. 1
0270-7306/07/$08.00+0     doi:10.1128/MCB.00561-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Targeted Deletion of the Muscular Dystrophy Gene myotilin Does Not Perturb Muscle Structure or Function in Mice{triangledown}

Monica Moza,1* Luca Mologni,1,{dagger} Ras Trokovic,2,{ddagger} Georgine Faulkner,3 Juha Partanen,2 and Olli Carpén1,4

Department of Pathology and Neuroscience Program, Biomedicum Helsinki, P.O. Box 63, Haartmaninkatu 8, 00014 University of Helsinki, Helsinki, Finland,1 Institute of Biotechnology, Viikki Biocenter, Developmental Biology Program, P.O. Box 56, Viikinkaari 9, 00014 University of Helsinki, Helsinki, Finland,2 International Center for Genetic Engineering and Biotechnology, Padriciano 99, Trieste, Italy,3 Department of Pathology, University of Turku, and Turku University Central Hospital, Kiinamyllynkatu 10, 20520 Turku, Finland4

Received 30 March 2006/ Returned for modification 27 May 2006/ Accepted 17 October 2006

Myotilin, palladin, and myopalladin form a novel small subfamily of cytoskeletal proteins that contain immunoglobulin-like domains. Myotilin is a thin filament-associated protein localized at the Z-disk of skeletal and cardiac muscle cells. The direct binding to F-actin, efficient cross-linking of actin filaments, and prevention of induced disassembly of filaments are key roles of myotilin that are thought to be involved in structural maintenance and function of the sarcomere. Missense mutations in the myotilin-encoding gene cause dominant limb girdle muscular dystrophy type 1A and spheroid body myopathy and are the molecular defect that can cause myofibrillar myopathy. Here we describe the generation and analysis of mice that lack myotilin, myo–/– mice. Surprisingly, myo–/– mice maintain normal muscle sarcomeric and sarcolemmal integrity. Also, loss of myotilin does not cause alterations in the heart or other organs of newborn or adult myo–/– mice. The mice develop normally and have a normal life span, and their muscle capacity does not significantly differ from wild-type mice even after prolonged physical stress. The results suggest that either myotilin does not participate in muscle development and basal function maintenance or other proteins serve as structural and functional compensatory molecules when myotilin is absent.

* Corresponding author. Mailing address: Neuroscience Program and Department of Pathology, Biomedicum Helsinki, Haartmaninkatu 8, P.O. Box 63, 00014 University of Helsinki, Helsinki, Finland. Phone: 358-9-19125652. Fax: 358-9-47171964. E-mail: monica.moza{at}helsinki.fi.

{triangledown} Published ahead of print on 30 October 2006.

{dagger} Present address: University of Milan-Bicocca, Milan, Italy.

{ddagger} Present address: Program of Developmental and Reproductive Biology, Biomedicum Helsinki, University of Helsinki, Helsinki, Finland.

Molecular and Cellular Biology, January 2007, p. 244-252, Vol. 27, No. 1
0270-7306/07/$08.00+0     doi:10.1128/MCB.00561-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.



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