HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) All Versions of this Article: fj.06-7659comv1 fj.06-7659comv2 21/8/1768    most recent Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Klinge, L. Articles by Bushby, K. Search for Related Content PubMed PubMed Citation Articles by Klinge, L. Articles by Bushby, K.

From T-tubule to sarcolemma: damage-induced dysferlin translocation in early myogenesis

University of Newcastle, Institute of Human Genetics, International Centre for Life, Newcastle-upon-Tyne, UK

¹Correspondence: Institute of Human Genetics, University of Newcastle upon Tyne, International Centre for Life, Central Pkwy, NE1 3BZ Newcastle upon Tyne, England, UK. E-mail: kate.bushby{at}ncl.ac.uk

The dysferlin gene is mutated in limb-girdle muscular dystrophy type 2B, Miyoshi myopathy, and distal anterior compartment myopathy. In mature skeletal muscle, dysferlin is located predominantly at the sarcolemma, where it plays a role in membrane fusion and repair. To investigate the role of dysferlin during early muscle differentiation, its localization was studied at high resolution in a muscle cell line. This demonstrated that dysferlin is not expressed at the plasmalemma of myotubes but mostly localizes to the T-tubule network. However, dysferlin translocated to the site of injury and toward the plasma membrane in a Ca²⁺-dependent fashion in response to a newly designed in vitro wounding assay. This reaction was specific to the full-length protein, as heterologously expressed deletion mutants of distinct C2 domains of dysferlin did not show this response. These results shed light on the dynamics of muscle membrane repair and are highly indicative of a specific role of dysferlin in this process in early myogenesis.—Klinge, L., Laval, S., Keers, S., Haldane, F., Straub, V., Barresi, R., Bushby, K. From T-tubule to sarcolemma: damage-induced dysferlin translocation in early myogenesis.

Key Words: membrane repair • muscular dystrophy • T-tubulogenesis

This article has been cited by other articles:

				D. J. Hernandez-Deviez, M. T. Howes, S. H. Laval, K. Bushby, J. F. Hancock, and R. G. Parton Caveolin Regulates Endocytosis of the Muscle Repair Protein, Dysferlin J. Biol. Chem., March 7, 2008; 283(10): 6476 - 6488. [Abstract] [Full Text] [PDF]

				R. L. Mellgren and X. Huang Fetuin A Stabilizes m-Calpain and Facilitates Plasma Membrane Repair J. Biol. Chem., December 7, 2007; 282(49): 35868 - 35877. [Abstract] [Full Text] [PDF]