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© The Rockefeller University Press, 0021-9525/1997//137 $5.00
The Journal of Cell Biology, Volume 136, Number 1, , 1997 137-154


Article

Caveolin-3 Associates with Developing T-tubules during Muscle Differentiation



Robert G. Parton*, Michael Way{ddagger}, Natasha Zorzi*, and Espen Stang*

* Centre for Microscopy and Microanalysis, Department of Physiology and Pharmacology, and Centre for Molecular and Cellular Biology, University of Queensland, Queensland 4072, Brisbane, Australia; and {ddagger} European Molecular Biology Laboratory, D69012 Heidelberg, Germany

Caveolae, flask-shaped invaginations of the plasma membrane, are particularly abundant in muscle cells. We have recently cloned a muscle-specific caveolin, termed caveolin-3, which is expressed in differentiated muscle cells. Specific antibodies to caveolin-3 were generated and used to characterize the distribution of caveolin-3 in adult and differentiating muscle. In fully differentiated skeletal muscle, caveolin-3 was shown to be associated exclusively with sarcolemmal caveolae. Localization of caveolin-3 during differentiation of primary cultured muscle cells and development of mouse skeletal muscle in vivo suggested that caveolin-3 is transiently associated with an internal membrane system. These elements were identified as developing transverse-(T)-tubules by double-labeling with antibodies to the {alpha}1 subunit of the dihydropyridine receptor in C2C12 cells. Ultrastructural analysis of the caveolin-3– labeled elements showed an association of caveolin-3 with elaborate networks of interconnected caveolae, which penetrated the depths of the muscle fibers. These elements, which formed regular reticular structures, were shown to be surface-connected by labeling with cholera toxin conjugates. The results suggest that caveolin-3 transiently associates with T-tubules during development and may be involved in the early development of the T-tubule system in muscle.


Abbreviations used in this paper: CT-B, cholera toxin binding subunit; DIG, detergent-insoluble glycosphingolipid-enriched complex; DHPR, dihydropyridine receptor; T-tubule, transverse-tubule.

Address all correspondence to R.G. Parton, Centre for Microscopy and Microanalysis, University of Queensland, Queensland 4072, Australia. Tel.: 61-7-3365-6468. Fax: 61-7-3365-4422. e-mail: R.Parton{at}mailbox.uq.oz.au



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