ArticleBiophysical journal2001
Binding of dystrophin's tandem calponin homology domain to F-actin is modulated by actin's structure.
Article in Biophysical journal, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 20 citations in OpenAlex.
- Multiple Mechanisms to Regulate Actin Functions: "Fundamental" Versus Lineage-Specific Mechanisms and Hierarchical Relationships.Biomolecules · 2025Review
- Article
- Dynamics of Dystrophin's Actin-Binding Domain.Biophysical journal · 2018Article
- Actin-microtubule coordination at growing microtubule ends.Nature communications · 2014Article
- Thermodynamic stability, unfolding kinetics, and aggregation of the N-terminal actin-binding domains of utrophin and dystrophin.Proteins · 2012Article
- Interaction of microtubules and actin with the N-terminus of βPix-b(L) directs cellular pinocytosis.Molecular and cellular biochemistry · 2011Article
- Actin binding domains direct actin-binding proteins to different cytoskeletal locations.BMC cell biology · 2008Article
- High-resolution cryo-EM structure of the F-actin-fimbrin/plastin ABD2 complex.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
- Myosin heavy-chain kinase A from Dictyostelium possesses a novel actin-binding domain that cross-links actin filaments.The Biochemical journal · 2006Article
- Specific interaction of the actin-binding domain of dystrophin with intermediate filaments containing keratin 19.Molecular biology of the cell · 2005Article
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
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.
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