ArticleThe Journal of biological chemistry2009
Smooth muscle heavy meromyosin phosphorylated on one of its two heads supports force and motion.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 29 citations in OpenAlex.
- Vascular Smooth Muscle Myosin 2 Filaments Dynamically Assemble and Stabilize During Induced Contractility.Arteriosclerosis, thrombosis, and vascular biology · 2026Article
- Vascular Smooth Muscle Myosin 2 Filaments Dynamically Assemble and Stabilize During Induced Contractility.bioRxiv : the preprint server for biology · 2026Article
- Modeling thick filament activation suggests a molecular basis for force depression.Biophysical journal · 2024Article
- MyosinA is a druggable target in the widespread protozoan parasite Toxoplasma gondii.PLoS biology · 2023Article
- Force-velocity and tension transient measurements from Drosophila jump muscle reveal the necessity of both weakly-bound cross-bridges and series elasticity in models of muscle contraction.Archives of biochemistry and biophysics · 2021Article
- The central role of the tail in switching off 10S myosin II activity.The Journal of general physiology · 2019Article
- Hypertrophic cardiomyopathy and the myosin mesa: viewing an old disease in a new light.Biophysical reviews · 2018Review
- Quantitative Determination of the Probability of Multiple-Motor Transport in Bead-Based Assays.Biophysical journal · 2016Article
- Tropomyosin controls sarcomere-like contractions for rigidity sensing and suppressing growth on soft matrices.Nature cell biology · 2016Article
- Vascular disease-causing mutation R258C in ACTA2 disrupts actin dynamics and interaction with myosin.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- The extent of cardiac myosin binding protein-C phosphorylation modulates actomyosin function in a graded manner.Journal of muscle research and cell motility · 2012Article
- Mechanical coupling between myosin molecules causes differences between ensemble and single-molecule measurements.Biophysical journal · 2012Article
- Phosphorylated smooth muscle heavy meromyosin shows an open conformation linked to activation.Journal of molecular biology · 2012Article
- Biochemistry of smooth muscle myosin light chain kinase.Archives of biochemistry and biophysics · 2011Review
- Cytokinesis through biochemical-mechanical feedback loops.Seminars in cell & developmental biology · 2010Review
- Modeling smooth muscle myosin's two heads: long-lived enzymatic roles and phosphorylation-dependent equilibria.Biophysical journal · 2010Article
- 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
- A mechanical model of actin stress fiber formation and substrate elasticity sensing in adherent cells.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- A small-molecule inhibitor of T. gondii motility induces the posttranslational modification of myosin light chain-1 and inhibits myosin motor activity.PLoS pathogens · 2010Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Smooth muscle myosin is activated by regulatory light chain (RLC) phosphorylation. In the unphosphorylated state the activity of both heads is suppressed due to an asymmetric, intramolecular interaction between the heads. The properties of myosin with only one of its two RLCs phosphorylated, a state likely to be present both during the activation and the relaxation phase of smooth muscle, is less certain despite much investigation. Here we further characterize the mechanical properties of an expressed heavy meromyosin (HMM) construct with only one of its RLCs phosphorylated (HMM-1P). This construct was previously shown to have more than 50% of the ATPase activity of fully phosphorylated myosin (HMM-2P) and to move actin at the same speed in a motility assay as HMM-2P (Rovner, A. S., Fagnant, P. M., and Trybus, K. M. (2006) Biochemistry 45, 5280-5289). Here we show that the unitary step size and attachment time to actin of HMM-1P is indistinguishable from that of HMM-2P. Force-velocity measurements on small ensembles show that HMM-1P can generate approximately half the force of HMM-2P, which may relate to the observed duty ratio of HMM-1P being approximately half that of HMM-2P. Therefore, single-phosphorylated smooth muscle HMM molecules are active species, and the head associated with the unphosphorylated RLC is mechanically competent, allowing it to make a substantial contribution to both motion and force generation during smooth muscle contraction.
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