spacer gif spacer gif spacer gif spacer gif spacer gif
QUICK SEARCH:   [advanced]


spacer gif
     Home     Help     Feedback     Subscriptions     Archive     Search     Table of Contents    

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
This Article
Right arrow Figures Only
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Supplementary Material
Right arrow All Versions of this Article:
jcs.021634v1
121/12/2062    most recent
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Related articles in JCS
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Google Scholar
Right arrow Articles by Hijikata, T.
Right arrow Articles by Yorifuji, H.
PubMed
Right arrow PubMed Citation
Right arrow Articles by Hijikata, T.
Right arrow Articles by Yorifuji, H.

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


Related articles in JCS:

β-Synemin muscles in

JCS 2008 121: 1203. [Full Text]  





© The Company of Biologists Ltd 2008