ArticleThe Journal of cell biology1989
Filamentous smooth muscle myosin is regulated by phosphorylation.
Article in The Journal of cell biology, 1989. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
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Who cites it
39 citing papers in PubMed, 107 citations in OpenAlex.
- DRAK2 regulates myosin light chain phosphorylation in T cells.Journal of cell science · 2024Article
- Article
- Self-assembly of smooth muscle myosin filaments: adaptation of filament length by telokin and Mg·ATP.European biophysics journal : EBJ · 2022Article
- Cryo-EM structure of the autoinhibited state of myosin-2.Science advances · 2021Article
- TheMolecular biology of the cell · 2020Article
- Cargo-Mediated Activation of Cytoplasmic DyneinFrontiers in cell and developmental biology · 2020Review
- Kinetic Adaptations of Myosins for Their Diverse Cellular Functions.Traffic (Copenhagen, Denmark) · 2016Review
- Various Themes of Myosin Regulation.Journal of molecular biology · 2016Review
- Molecular model for force production and transmission during vertebrate gastrulation.Development (Cambridge, England) · 2016Article
- Highly sensitive myosin phosphorylation analysis in the renal afferent arteriole.Journal of smooth muscle research = Nihon Heikatsukin Gakkai kikanshi · 2016Review
- The kinetics underlying the velocity of smooth muscle myosin filament sliding on actin filaments in vitro.The Journal of biological chemistry · 2014Article
- Myosin light chains: Teaching old dogs new tricks.Bioarchitecture · 2014Review
- Mammalian myosin-18A, a highly divergent myosin.The Journal of biological chemistry · 2013Article
- Affinity for MgADP and force of unbinding from actin of myosin purified from tonic and phasic smooth muscle.American journal of physiology. Cell physiology · 2008Article
- Estrogen modulation of MgATPase activity of nonmuscle myosin-II-B filaments.Endocrinology · 2007Article
- Folding and regulation in myosins II and V.Journal of muscle research and cell motility · 2007Review
- Phosphorylation of a single head of smooth muscle myosin activates the whole molecule.Biochemistry · 2006Article
- Rho-kinase contributes to diphosphorylation of myosin II regulatory light chain in nonmuscle cells.Oncogene · 2002Article
- A structural model for phosphorylation control of Dictyostelium myosin II thick filament assembly.The Journal of cell biology · 1999Article
- Unphosphorylated crossbridges and latch: smooth muscle regulation revisited.Journal of muscle research and cell motility · 1999Article
Corrections and comments
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Authors and funding
1 author at 1 institution in 1 country.
Funding
Abstract
The enzymatic activity of filamentous dephosphorylated smooth muscle myosin has been difficult to determine because the polymer disassembles to the folded conformation in the presence of MgATP. Monoclonal antirod antibodies were used here to "fix" dephosphorylated myosin in the filamentous state. The steady-state actin-activated ATPase of phosphorylated filaments was 30-100-fold higher than that of antibody-stabilized dephosphorylated filaments, suggesting that phosphorylation can activate ATPase activity independent of changes in assembly. The degree of regulation may exceed 100-fold, because steady-state measurements slightly overestimate the rate of product release from dephosphorylated filaments. Single-turnover experiments in the absence of actin showed that although dephosphorylated folded myosin released products at the low rate of 0.0005 s-1 (Cross, R. A., K. E. Cross, A. Sobieszek. 1986. EMBO [Eur. Mol. Biol. Organ.] J. 5:2637-2641) the rate of product release from dephosphorylated filaments was only 3-12-fold higher, depending on the ionic strength. The addition of actin did not increase this rate to any appreciable extent. Dephosphorylated filaments and dephosphorylated heavy meromyosin (Sellers, J. R. 1985. J. Biol. Chem. 260:15815-15819) thus have similar low rates of phosphate release both in the presence and absence of actin. These results show that light chain phosphorylation alone, without invoking other mechanisms, is an effective switch for regulating the activity of smooth muscle myosin filaments.
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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.