ArticleProceedings of the National Academy of Sciences of the United States of America2009
Dystrophin and utrophin have distinct effects on the structural dynamics of actin.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 41 citations in OpenAlex.
- CRISPR-Cas9-mediated upregulation of utrophin ameliorates Duchenne muscular dystrophy.Molecular therapy : the journal of the American Society of Gene Therapy · 2026Article
- 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
- Microutrophin expression in dystrophic mice displays myofiber type differences in therapeutic effects.PLoS genetics · 2020Article
- Human cardiac myosin-binding protein C restricts actin structural dynamics in a cooperative and phosphorylation-sensitive manner.The Journal of biological chemistry · 2019Article
- Nuclear Actin: From Discovery to Function.Anatomical record (Hoboken, N.J. : 2007) · 2018Review
- Dynamics of Dystrophin's Actin-Binding Domain.Biophysical journal · 2018Article
- A Genome-Wide Association Study IdentifiesPsychiatry investigation · 2017Article
- Utrophin Compensates dystrophin Loss during Mouse Spermatogenesis.Scientific reports · 2017Article
- Structural Interface Forms and Their Involvement in Stabilization of Multidomain Proteins or Protein Complexes.International journal of molecular sciences · 2016Article
- Article
- The pros and cons of common actin labeling tools for visualizing actin dynamics during Drosophila oogenesis.Developmental biology · 2014Article
- Muscle lim protein isoform negatively regulates striated muscle actin dynamics and differentiation.The FEBS journal · 2014Article
- The potential of sarcospan in adhesion complex replacement therapeutics for the treatment of muscular dystrophy.The FEBS journal · 2013Review
- The structural dynamics of actin during active interaction with myosin depends on the isoform of the essential light chain.Biochemistry · 2013Article
- Cardiac myosin binding protein-C restricts intrafilament torsional dynamics of actin in a phosphorylation-dependent manner.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Structural dynamics of muscle protein phosphorylation.Journal of muscle research and cell motility · 2012Review
- Myosin and tropomyosin stabilize the conformation of formin-nucleated actin filaments.The Journal of biological chemistry · 2012Article
- Impacts of dystrophin and utrophin domains on actin structural dynamics: implications for therapeutic design.Journal of molecular biology · 2012Article
- Thermodynamic stability, unfolding kinetics, and aggregation of the N-terminal actin-binding domains of utrophin and dystrophin.Proteins · 2012Article
- The carboxy-terminal third of dystrophin enhances actin binding activity.Journal of molecular biology · 2012Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
We have used time-resolved spectroscopy to investigate the structural dynamics of actin interaction with dystrophin and utrophin in relationship to the pathology of muscular dystrophy. Dystrophin and utrophin bind actin in vitro with similar affinities, but the molecular contacts of these two proteins with actin are different. It has been hypothesized that the presence of two low-affinity actin-binding sites in dystrophin allows more elastic response of the actin-dystrophin-sarcolemma linkage to muscle stretches, compared with utrophin, which binds via one contiguous actin-binding domain. We have directly tested this hypothesis by determining the effects of dystrophin and utrophin on the microsecond rotational dynamics of a phosphorescent dye attached to C374 on actin, as detected by transient phosphorescence anisotropy (TPA). Binding of dystrophin or utrophin to actin resulted in significant changes in the TPA decay, increasing the final anisotropy (restricting the rotational amplitude) and decreasing the rotational correlation times (increasing the rotational rates and the torsional flexibility). This paradoxical combination of effects on actin dynamics (decreased amplitude but increased rate) has not been observed for other actin-binding proteins. Thus, when dystrophin or utrophin binds, actin becomes less like cast iron (strong but brittle) and more like steel (stronger and more resilient). At low levels of saturation, the binding of dystrophin and utrophin has similar effects, but at higher levels, utrophin caused much greater restrictions in amplitude and increases in rate. The effects of dystrophin and utrophin on actin dynamics provide molecular insight into the pathology of muscular dystrophy.
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Registered trials
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