ArticleProceedings of the National Academy of Sciences of the United States of America2005
Site-directed spin labeling reveals a conformational switch in the phosphorylation domain of smooth muscle myosin.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed.
- 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
- Myosin lever arm orientation in muscle determined with high angular resolution using bifunctional spin labels.The Journal of general physiology · 2019Article
- Article
- Tarantula myosin free head regulatory light chain phosphorylation stiffens N-terminal extension, releasing it and blocking its docking back.Molecular bioSystems · 2015Article
- Sequential myosin phosphorylation activates tarantula thick filament via a disorder-order transition.Molecular bioSystems · 2015Article
- Towards the computational design of protein post-translational regulation.Bioorganic & medicinal chemistry · 2015Review
- Effects of pseudophosphorylation mutants on the structural dynamics of smooth muscle myosin regulatory light chain.Molecular bioSystems · 2014Article
- Role of the essential light chain in the activation of smooth muscle myosin by regulatory light chain phosphorylation.Journal of structural biology · 2014Article
- Physicochemical mechanisms of protein regulation by phosphorylation.Frontiers in genetics · 2014Review
- Electron paramagnetic resonance analysis of the vimentin tail domain reveals points of order in a largely disordered region and conformational adaptation upon filament assembly.Protein science : a publication of the Protein Society · 2013Article
- Structural dynamics of muscle protein phosphorylation.Journal of muscle research and cell motility · 2012Review
- CLC anion channel regulatory phosphorylation and conserved signal transduction domains.Biophysical journal · 2012Article
- Broad disorder and the allosteric mechanism of myosin II regulation by phosphorylation.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- Characterization of the disordered-to-α-helical transition of IA₃ by SDSL-EPR spectroscopy.Protein science : a publication of the Protein Society · 2011Article
- Nonmuscle myosin IIA with a GFP fused to the N-terminus of the regulatory light chain is regulated normally.Journal of muscle research and cell motility · 2010Article
- Common structural motifs for the regulation of divergent class II myosins.The Journal of biological chemistry · 2010Review
- Phosphorylation-induced structural changes in smooth muscle myosin regulatory light chain.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- Kinetic and motor functions mediated by distinct regions of the regulatory light chain of smooth muscle myosin.Biochimica et biophysica acta · 2009Article
- Site-directed spectroscopic probes of actomyosin structural dynamics.Annual review of biophysics · 2009Review
- Three-dimensional reconstruction of tarantula myosin filaments suggests how phosphorylation may regulate myosin activity.Journal of molecular biology · 2008Article
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4 authors.
Funding
Abstract
We have used site-directed spin labeling and EPR spectroscopy to detect structural changes within the regulatory light chain (RLC) of smooth muscle myosin upon phosphorylation. Smooth muscle contraction is activated by phosphorylation of S19 on RLC, but the structural basis of this process is unknown. There is no crystal structure containing a phosphorylated RLC, and there is no crystal structure for the N-terminal region of any RLC. Therefore, we have prepared single-Cys mutations throughout RLC, exchanged each mutant onto smooth muscle heavy meromyosin, verified normal regulatory function, and used EPR to determine dynamics and solvent accessibility at each site. A survey of spin-label sites throughout the RLC revealed that only the N-terminal region (first 24 aa) shows a significant change in dynamics upon phosphorylation, with most of the first 17 residues showing an increase in rotational amplitude. Therefore, we focused on this N-terminal region. Additional structural information was obtained from the pattern of oxygen accessibility along the sequence. In the absence of phosphorylation, little or no periodicity was observed, suggesting a lack of secondary structural order in this region. However, phosphorylation induced a strong helical pattern (3.6-residue periodicity) in the first 17 residues, while increasing accessibility throughout the first 24 residues. We have identified a domain within RLC, the N-terminal phosphorylation domain, in which phosphorylation increases helical order, internal dynamics, and accessibility. These results support a model in which this disorder-to-order transition within the phosphorylation domain results in decreased head-head interactions, activating myosin in smooth muscle.
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