ArticleBiochemistry2006
Phosphorylation of a single head of smooth muscle myosin activates the whole molecule.
Article in Biochemistry, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 18 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
- Hypertrophic cardiomyopathy and the myosin mesa: viewing an old disease in a new light.Biophysical reviews · 2018Review
- Graded effects of unregulated smooth muscle myosin on intestinal architecture, intestinal motility and vascular function in zebrafish.Disease models & mechanisms · 2016Article
- Mechanisms of Vascular Smooth Muscle Contraction and the Basis for Pharmacologic Treatment of Smooth Muscle Disorders.Pharmacological reviews · 2016Review
- Collective dynamics of elastically coupled myosin V motors.The Journal of biological chemistry · 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
- Simultaneous observation of tail and head movements of myosin V during processive motion.The Journal of biological chemistry · 2010Article
- 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
- Modification of loop 1 affects the nucleotide binding properties of Myo1c, the adaptation motor in the inner ear.Biochemistry · 2010Article
- Smooth muscle heavy meromyosin phosphorylated on one of its two heads supports force and motion.The Journal of biological chemistry · 2009Article
- Smooth muscle myosin phosphorylated at single head shows sustained mechanical activity.The Journal of biological chemistry · 2008Article
- Molecular dynamics simulations reveal a disorder-to-order transition on phosphorylation of smooth muscle myosin.Biophysical journal · 2007Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Regulatory light chain (RLC) phosphorylation activates smooth and non-muscle myosin II, but it has not been established if phosphorylation of one head turns on the whole molecule. Baculovirus expression and affinity chromatography were used to isolate heavy meromyosin (HMM) containing one phosphorylated and one dephosphorylated RLC (1-P HMM). Motility and steady-state ATPase assays indicated that 1-P HMM is nearly as active as HMM with two phosphorylated heads (2-P HMM). Single-turnover experiments further showed that both the dephosphorylated and phosphorylated heads of 1-P HMM can be activated by actin. Singly phosphorylated full-length myosin was also an active species with two cycling heads. Our results suggest that phosphorylation of one RLC abolishes the asymmetric inhibited state formed by dephosphorylated myosin [Liu, J., et al. (2003) J. Mol. Biol. 329, 963-972], allowing activation of both the phosphorylated and dephosphorylated heads. These findings help explain how smooth muscles are able to generate high levels of stress with low phosphorylation levels.
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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.