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First published online 23 April 2003
doi: 10.1242/jcs.00422

This Article Figures Only Full Text Full Text (PDF) All Versions of this Article: jcs.00422v1 116/11/2261    most recent 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 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 Oh, S. W. Articles by Luna, E. J. Search for Related Content PubMed PubMed Citation Articles by Oh, S. W. Articles by Luna, E. J.

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^¶

Department of Cell Biology, University of Massachusetts Medical School, Worcester, MA 01655, USA
^* Present address: Central Research Institute of BodiTech, Inc. Chuncheon, Kangwon-Do 200-160, South Korea
Present address: Department of Biological Sciences, Indiana University South Bend, South Bend, IN 46634, USA
Present address: Department of Infection and Immunity, The Walter and Eliza Hall Institute of Medical Research, VIC 3050, Australia

^¶ Author for correspondence (e-mail: elizabeth.luna{at}umassmed.edu)

Accepted 11 February 2003

The membrane skeleton protein supervillin binds tightly to both F-actin and membranes and can potentiate androgen receptor activity in non-muscle cells. We report that muscle, which constitutes the principal tissue source for supervillin sequences, contains a 250 kDa isoform of supervillin that localizes within nuclei and with dystrophin at costameres, regions of F-actin membrane attachment in skeletal muscle. The gene encoding this protein, `archvillin' (Latin, archi; Greek, árchos; `principal' or `chief'), contains an evolutionarily conserved, muscle-specific 5' leader sequence. Archvillin cDNAs also contain four exons that encode 47 kDa of additional muscle-specific protein sequence in the form of two inserts within the function-rich N-terminus of supervillin. The first of these muscle-specific inserts contains two conserved nuclear targeting signals in addition to those found in sequences shared with supervillin. Archvillin, like supervillin, binds directly to radiolabeled F-actin and co-fractionates with plasma membranes. Colocalization of archvillin with membrane-associated actin filaments, non-muscle myosin II, and – to a lesser extent – vinculin was observed in myoblasts. Striking localizations of archvillin protein and mRNA were observed at the tips of differentiating myotubes. Transfected protein chimeras containing archvillin insert sequences inhibited myotube formation, consistent with a dominant-negative effect during early myogenesis. These data suggest that archvillin is among the first costameric proteins to assemble during myogenesis and that it contributes to myogenic membrane structure and differentiation.

Key words: Costamere, Sarcolemma, Membrane skeleton, C2C12 cells, 50MB-1 cells

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