NDLI: Binding of dystrophin's tandem calponin homology domain to F-actin is modulated by actin's structure.

Content Provider	PubMed Central
Author	Orlova, A. Prochniewicz, E. Thomas, D. D. Ervasti, J. M. Egelman, E. H. Rybakova, I. N.
Abstract	Dystrophin has been shown to be associated in cells with actin bundles. Dys-246, an N-terminal recombinant protein encoding the first 246 residues of dystrophin, includes two calponin-homology (CH) domains, and is similar to a large class of F-actin cross-linking proteins including alpha-actinin, fimbrin, and spectrin. It has been shown that expression or microinjection of amino-terminal fragments of dystrophin or the closely related utrophin resulted in the localization of these protein domains to actin bundles. However, in vitro studies have failed to detect any bundling of actin by either intact dystrophin or Dys-246. We show here that the structure of F-actin can be modulated so that there are two modes of Dys-246 binding, from bundling actin filaments to only binding to single filaments. The changes in F-actin structure that allow Dys-246 to bundle filaments are induced by covalent modification of Cys-374, proteolytic cleavage of F-actin's C-terminus, mutation of yeast actin's N-terminus, and different buffers. The present results suggest that F-actin's structural state can have a large influence on the nature of actin's interaction with other proteins, and these different states need to be considered when conducting in vitro assays.
Related Links	http://dx.doi.org/10.1016/s0006-3495(01)76162-0
Ending Page	1931
Page Count	6
Starting Page	1926
File Format	PDF
ISSN	00063495
e-ISSN	15420086
Journal	Biophysical Journal
Issue Number	4
Volume Number	80
Language	English
Publisher Date	2001-04-01
Access Restriction	Open
Subject Keyword	Biophysics Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Biophysics

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The N-Terminal Actin-Binding Tandem Calponin-Homology (CH) Domain of Dystrophin Is in a Closed Conformation in Solution and When Bound to F-actin

Steric Regulation of Tandem Calponin Homology Domain Actin-Binding Affinity

Dystrophin’s Tandem Calponin-Homology Domains: Is the Case Closed?

Large-scale opening of utrophin’s tandem calponin homology (CH) domains upon actin binding by an induced-fit mechanism

Opening of tandem calponin homology domains regulates their affinity for F-actin

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Three-dimensional reconstruction of a co-complex of F-actin with antibody Fab fragments to actin's NH2 terminus.

Binding of dystrophin's tandem calponin homology domain to F-actin is modulated by actin's structure.

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