ArticleProceedings of the National Academy of Sciences of the United States of America2011
Large-scale opening of utrophin's tandem calponin homology (CH) domains upon actin binding by an induced-fit mechanism.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 43 citations in OpenAlex.
- In silico conformational dynamics of the α-actinin-2 actin-binding domain upon phosphorylation.Biophysical journal · 2026Article
- Human Plastins are Novel Cytoskeletal pH Sensors with a Reduced F-actin Bundling Capacity at Basic pH.Journal of molecular biology · 2025Article
- Paralemmin-1 controls the nanoarchitecture of the neuronal submembrane cytoskeleton.Science advances · 2025Article
- Structural Dynamics of Protein Interactions Using Site-Directed Spin Labeling of Cysteines to Measure Distances and Rotational Dynamics with EPR Spectroscopy.Applied magnetic resonance · 2024Article
- Cardiomyocyte external mechanical unloading activates modifications of α-actinin differently from sarcomere-originated unloading.The FEBS journal · 2023Article
- Structure of the Lifeact-F-actin complex.PLoS biology · 2020Article
- Structural insights into actin filament recognition by commonly used cellular actin markers.The EMBO journal · 2020Article
- Article
- Steric regulation of tandem calponin homology domain actin-binding affinity.Molecular biology of the cell · 2019Article
- Structural basis of the filamin A actin-binding domain interaction with F-actin.Nature structural & molecular biology · 2018Article
- Dynamics of Dystrophin's Actin-Binding Domain.Biophysical journal · 2018Article
- Structural dynamics of calmodulin-ryanodine receptor interactions: electron paramagnetic resonance using stereospecific spin labels.Scientific reports · 2018Article
- Molecular and cytoskeletal regulations in epidermal development.Seminars in cell & developmental biology · 2017Review
- 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
- A human β-III-spectrin spinocerebellar ataxia type 5 mutation causes high-affinity F-actin binding.Scientific reports · 2016Article
- F-actin clustering and cell dysmotility induced by the pathological W148R missense mutation of filamin B at the actin-binding domain.American journal of physiology. Cell physiology · 2016Article
- Impact of methionine oxidation on calmodulin structural dynamics.Biochemical and biophysical research communications · 2015Article
- Optimization of bicelle lipid composition and temperature for EPR spectroscopy of aligned membranes.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2015Article
- Binding to F-actin guides cadherin cluster assembly, stability, and movement.The Journal of cell biology · 2013Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
We have used site-directed spin labeling and pulsed electron paramagnetic resonance to resolve a controversy concerning the structure of the utrophin-actin complex, with implications for the pathophysiology of muscular dystrophy. Utrophin is a homolog of dystrophin, the defective protein in Duchenne and Becker muscular dystrophies, and therapeutic utrophin derivatives are currently being developed. Both proteins have a pair of N-terminal calponin homology (CH) domains that are important for actin binding. Although there is a crystal structure of the utrophin actin-binding domain, electron microscopy of the actin-bound complexes has produced two very different structural models, in which the CH domains are in open or closed conformations. We engineered a pair of labeling sites in the CH domains of utrophin and used dipolar electron-electron resonance to determine the distribution of interdomain distances with high resolution. We found that the two domains are flexibly connected in solution, indicating a dynamic equilibrium between two distinct open structures. Upon actin binding, the two domains become dramatically separated and ordered, indicating a transition to a single open and extended conformation. There is no trace of this open conformation of utrophin in the absence of actin, providing strong support for an induced-fit model of actin binding.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.