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Journal of Cell Science, Vol 107, Issue 6 1469-1475, Copyright © 1994 by Company of Biologists

JOURNAL ARTICLES

Independent localization of dystrophin N- and C-terminal regions to the sarcolemma of mdx mouse myofibres in vivo

MG Dunckley, KE Wells, TA Piper, DJ Wells and G Dickson
Department of Experimental Pathology, UMDS, Guy's Hospital, London, UK.

Dystrophin has been proposed to associate with the skeletal muscle membrane by way of a glycoprotein complex that interacts with its C-terminal domains. Transfection of mdx mouse myotubes in culture or myofibres in vivo with recombinant genes encoding human dystrophin deletion mutants shows, however, that not only the C terminus of dystrophin but also its N-terminal actin-binding domain can locate independently to the muscle sarcolemma. This observation suggests that lack of sarcolemma-associated dystrophin in Duchenne muscular dystrophy (DMD) muscle may result from enhanced degradation of truncated mutation products rather than their inability per se to associate with the sarcolemma.




© The Company of Biologists Ltd 1994