ArticleJournal of molecular biology2012
Phosphorylated smooth muscle heavy meromyosin shows an open conformation linked to activation.
Article in Journal of molecular biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
21 citing papers in PubMed, 28 citations in OpenAlex.
- Spatial control of myosin regulatory light chain phosphorylation modulates cardiac thick filament mechanosensing.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
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- Synthetic biology approaches to dissecting linear motor protein function: towards the design and synthesis of artificial autonomous protein walkers.Biophysical reviews · 2020Review
- Tyrosine Phosphorylation of the Myosin Regulatory Light Chain Controls Non-muscle Myosin II Assembly and Function in Migrating Cells.Current biology : CB · 2020Article
- Molecular interaction site on procoagulant myosin for factor Xa-dependent prothrombin activation.The Journal of biological chemistry · 2019Article
- Piperine, an alkaloid inhibiting the super-relaxed state of myosin, binds to the myosin regulatory light chain.Archives of biochemistry and biophysics · 2018Article
- Phosphorylation of the regulatory light chain of myosin in striated muscle: methodological perspectives.European biophysics journal : EBJ · 2016Review
- Myosin light chain kinase steady-state kinetics: comparison of smooth muscle myosin II and nonmuscle myosin IIB as substrates.Cell biochemistry and function · 2016Article
- Made to measure - keeping Rho kinase at a distance.Small GTPases · 2016Review
- Conserved Intramolecular Interactions Maintain Myosin Interacting-Heads Motifs Explaining Tarantula Muscle Super-Relaxed State Structural Basis.Journal of molecular biology · 2016Article
- The Relay/Converter Interface Influences Hydrolysis of ATP by Skeletal Muscle Myosin II.The Journal of biological chemistry · 2016Article
- Article
- A role for the Ca(2+)-dependent tyrosine kinase Pyk2 in tonic depolarization-induced vascular smooth muscle contraction.Journal of muscle research and cell motility · 2015Review
- Phosphorylation of myosin regulatory light chain controls myosin head conformation in cardiac muscle.Journal of molecular and cellular cardiology · 2015Article
- Sequential myosin phosphorylation activates tarantula thick filament via a disorder-order transition.Molecular bioSystems · 2015Article
- Role of the essential light chain in the activation of smooth muscle myosin by regulatory light chain phosphorylation.Journal of structural biology · 2014Article
- Myosin light chains: Teaching old dogs new tricks.Bioarchitecture · 2014Review
- Structural basis of the relaxed state of a Ca2+-regulated myosin filament and its evolutionary implications.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Modification of interface between regulatory and essential light chains hampers phosphorylation-dependent activation of smooth muscle myosin.The Journal of biological chemistry · 2012Article
- Structure, interactions and function of the N-terminus of cardiac myosin binding protein C (MyBP-C): who does what, with what, and to whom?Journal of muscle research and cell motility · 2012Review
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
Abstract
Smooth muscle myosin and smooth muscle heavy meromyosin (smHMM) are activated by regulatory light chain phosphorylation, but the mechanism remains unclear. Dephosphorylated, inactive smHMM assumes a closed conformation with asymmetric intramolecular head-head interactions between motor domains. The "free head" can bind to actin, but the actin binding interface of the "blocked head" is involved in interactions with the free head. We report here a three-dimensional structure for phosphorylated, active smHMM obtained using electron crystallography of two-dimensional arrays. Head-head interactions of phosphorylated smHMM resemble those found in the dephosphorylated state but occur between different molecules, not within the same molecule. The light chain binding domain structure of phosphorylated smHMM differs markedly from that of the "blocked" head of dephosphorylated smHMM. We hypothesize that regulatory light chain phosphorylation opens the inhibited conformation primarily by its effect on the blocked head. Singly phosphorylated smHMM is not compatible with the closed conformation if the blocked head is phosphorylated. This concept has implications for the extent of myosin activation at low levels of phosphorylation in smooth muscle.
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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.