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Biochim Biophys Acta. 2010 Sep;1804(9):1713-22. doi: 10.1016/j.bbapap.2010.05.001. Epub 2010 May 21.

Dystrophin: more than just the sum of its parts.

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  • 1Université de Rennes 1, UMR CNRS 6026 Interactions cellulaires et moléculaires, Equipe RMN et Interactions lipides-protéines, IFR 140, Faculté de Médecine, CS 34317, 35043 Rennes cedex, France. elisabeth.lerumeur@univ-rennes1.fr

Abstract

Dystrophin is one of a number of large cytoskeleton associated proteins that connect between various cytoskeletal elements and often are tethered to the membrane through other transmembrane protein complexes. These cytolinker proteins often provide structure and support to the cells where they are expressed, and mutations in genes encoding these proteins frequently gives rise to disease. Dystrophin is no exception in any of these respects, providing connections between a transmembrane complex known as the dystrophin-glycoprotein complex and the underlying cytoskeleton. The most established connection and possibly the most important is that to F-actin, but more recently evidence has been forthcoming of connections to membrane phospholipids, intermediate filaments and microtubules. Moreover it is becoming increasingly clear that the multiple spectrin-like repeats in the centre of the molecule, that had hitherto been thought to be largely redundant, harbour binding activities that have a significant impact on dystrophin functionality. This functionality is particularly apparent when assessed by the ability to rescue the dystrophic phenotype in mdx mice. This review will focus on the relatively neglected but functionally vital coiled-coil region of dystrophin, highlighting the structural relationships and interactions of the coiled-coil region and providing new insights into the functional role of this region.

Copyright © 2010 Elsevier B.V. All rights reserved.

PMID:
20472103
[PubMed - indexed for MEDLINE]
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