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Archvillin: criminal mastermind in myogenesis?

Membrane proteins connected to the cytoskeleton are essential for maintaining the integrity of the muscle plasma membrane under mechanical stress. The filamentous costamere lattice is particularly important for resisting lateral forces. It contains a variety of proteins, including ankyrin, dystrophin, integrins and spectrin, but critical organizing components have proven elusive. Elizabeth Luna and co-workers now reveal a potential mastermind behind the operation: archvillin (see p. 2261). Archvillin is a novel, muscle-specific isoform of supervillin, an actin-bundling protein that is implicated in actin-membrane linkage and shares some similarity with the microvillar protein villin. The authors show that archvillin is present at costameres in skeletal muscle and cofractionates with the plasma membrane. They also show that it can bind to actin, associates with actin filaments in vivo and localizes to the tips of differentiating myotubes. Perhaps their most important observation, however, is that a dominant negative archvillin mutant containing the insert sequences that distinguish it from supervillin can block myotube formation. This novel cytoskeletal linker thus appears to be important for both muscle architecture and differentiation.

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Archvillin, a muscle-specific isoform of supervillin, is an early expressed component of the costameric membrane skeleton

Sang W. Oh, Robert K. Pope, Kelly P. Smith, Jessica L. Crowley, Thomas Nebl, Jeanne B. Lawrence, and Elizabeth J. Luna
JCS 2003 116: 2261-2275. [Abstract] [Full Text]  

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Related articles in JCS Similar articles in this journal Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via Google Scholar Google Scholar Search for Related Content Social Bookmarking                         What's this?