ArticleFEBS open bio2012
Utrophin ABD binds to F-actin in an open conformation.
Article in FEBS open bio, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 14 citations in OpenAlex.
- The role of the dystrophin glycoprotein complex in muscle cell mechanotransduction.Communications biology · 2022Review
- Structural insights into actin filament recognition by commonly used cellular actin markers.The EMBO journal · 2020Article
- Article
- Structural basis of the filamin A actin-binding domain interaction with F-actin.Nature structural & molecular biology · 2018Article
- Spectraplakin family proteins - cytoskeletal crosslinkers with versatile roles.Journal of cell science · 2017Review
- In vivo epidermal migration requires focal adhesion targeting of ACF7.Nature communications · 2016Article
- 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.Biophysical journal · 2012Article
Corrections and comments
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Authors and funding
3 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Structural analyses of actin binding regions comprising tandem calponin homology domains alone and when bound to F-actin have revealed a number of different conformations with calponin homology domains in 'open' and 'closed' positions. In an attempt to resolve these issues we have examined the properties of the utrophin actin binding domain in open and closed conformations in order to verify the conformation when bound to F-actin. Locking the actin binding domain in a closed conformation using engineered cysteine residues in each calponin homology domain reduced the affinity for F-actin without affecting the stoichiometry furthermore differential scanning calorimetry experiments revealed a reduction in melting temperature on binding to actin. The data suggest the amino-terminal utrophin actin binding domain is in an open conformation in solution and when bound to F-actin.
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Registered trials
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