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First published online 27 May 2008
doi: 10.1242/jcs.021634

Journal of Cell Science 121, 2062-2074 (2008)
Published by The Company of Biologists 2008
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Research Article

Plectin 1 links intermediate filaments to costameric sarcolemma through β-synemin, {alpha}-dystrobrevin and actin

Takao Hijikata1,*, Akio Nakamura2, Keitaro Isokawa3, Michihiro Imamura4, Katsutoshi Yuasa1, Ryoki Ishikawa2, Kazuhiro Kohama2, Shinichi Takeda4 and Hiroshi Yorifuji5

1 Department of Anatomy and Cell Biology, Faculty of Pharmacy, Research Institute of Pharmaceutical Sciences, Musashino University, Tokyo 202-8585, Japan
2 Department of Molecular and Cellular Pharmacology, Gunma University Graduate School of Medicine, Gunma 371-8511, Japan
3 Department of Anatomy, Nihon University School of Dentistry, Tokyo 101-8310, Japan
4 Department of Molecular Therapy, National Institute of Neuroscience, NCNP, Tokyo 187-8502, Japan
5 Department of Anatomy, Gunma University Graduate School of Medicine, Gunma 371-8511, Japan

* Author for correspondence (e-mail: hijikata{at}musashino-u.ac.jp)

Accepted 19 March 2008

In skeletal muscles, the sarcolemma is possibly stabilized and protected against contraction-imposed stress by intermediate filaments (IFs) tethered to costameric sarcolemma. Although there is emerging evidence that plectin links IFs to costameres through dystrophin-glycoprotein complexes (DGC), the molecular organization from plectin to costameres still remains unclear. Here, we show that plectin 1, a plectin isoform expressed in skeletal muscle, can interact with β-synemin, actin and a DGC component, {alpha}-dystrobrevin, in vitro. Ultrastructurally, β-synemin molecules appear to be incorporated into costameric dense plaques, where they seem to serve as actin-associated proteins rather than IF proteins. In fact, they can bind actin and {alpha}-dystrobrevin in vitro. Moreover, in vivo immunoprecipitation analyses demonstrated that β-synemin- and plectin-immune complexes from lysates of muscle light microsomes contained {alpha}-dystrobrevin, dystrophin, nonmuscle actin, metavinculin, plectin and β-synemin. These findings suggest a model in which plectin 1 interacts with DGC and integrin complexes directly, or indirectly through nonmuscle actin and β-synemin within costameres. The DGC and integrin complexes would cooperate to stabilize and fortify the sarcolemma by linking the basement membrane to IFs through plectin 1, β-synemin and actin. Besides, the two complexes, together with plectin and IFs, might have their own functions as platforms for distinct signal transduction.

Key words: Costamere, Dystrobrevin, Dystrophin-glycoprotein complex, Plectin, Synemin


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JCS 2008 121: 1203. [Full Text]  





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