ArticleThe Journal of cell biology1994
Coupling of ATPase activity and motility in smooth muscle myosin is mediated by the regulatory light chain.
Article in The Journal of cell biology, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 78 citations in OpenAlex.
- The regulatory protein 14-3-3β binds to the IQ motifs of myosin-IC independent of phosphorylation.The Journal of biological chemistry · 2020Article
- Using the SpyTag SpyCatcher system to label smooth muscle myosin II filaments with a quantum dot on the regulatory light chain.Cytoskeleton (Hoboken, N.J.) · 2019Article
- Cloning, expression, and characterization of a novel molecular motor, Leishmania myosin-XXI.The Journal of biological chemistry · 2012Article
- Modification of interface between regulatory and essential light chains hampers phosphorylation-dependent activation of smooth muscle myosin.The Journal of biological chemistry · 2012Article
- Single myosin cross-bridge orientation in cardiac papillary muscle detects lever-arm shear strain in transduction.Biochemistry · 2011Article
- The on-off switch in regulated myosins: different triggers but related mechanisms.Journal of molecular biology · 2009Article
- Kinetic and motor functions mediated by distinct regions of the regulatory light chain of smooth muscle myosin.Biochimica et biophysica acta · 2009Article
- An unusual transduction pathway in human tonic smooth muscle myosin.Biophysical journal · 2007Article
- Trifluoperazine inhibits the MgATPase activity and in vitro motility of conventional and unconventional myosins.Journal of muscle research and cell motility · 2003Article
- In vivo observations of myosin II dynamics support a role in rear retraction.Molecular biology of the cell · 1999Article
- Expression of chicken gizzard RLC complements the cytokinesis and developmental defects of Dictyostelium RLC null cells.Journal of muscle research and cell motility · 1999Article
- Myosin conformational states determined by single fluorophore polarization.Proceedings of the National Academy of Sciences of the United States of America · 1998Article
- Myosin light chain-activating phosphorylation sites are required for oogenesis in Drosophila.The Journal of cell biology · 1997Article
- Slow cycling of unphosphorylated myosin is inhibited by calponin, thus keeping smooth muscle relaxed.Proceedings of the National Academy of Sciences of the United States of America · 1997Article
- A fluorescent protein biosensor of myosin II regulatory light chain phosphorylation reports a gradient of phosphorylated myosin II in migrating cells.Molecular biology of the cell · 1995Article
- Role of essential light chain EF hand domains in calcium binding and regulation of scallop myosin.Proceedings of the National Academy of Sciences of the United States of America · 1995Article
- Role of skeletal and smooth muscle myosin light chains.Biophysical journal · 1995Review
- Targeted disruption of the Dictyostelium RMLC gene produces cells defective in cytokinesis and development.The Journal of cell biology · 1994Article
- Regulation of Dictyostelium myosin II by phosphorylation: what is essential and what is important?The Journal of cell biology · 1994Review
- Role of myosin light chains.Journal of muscle research and cell motility · 1994Review
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Smooth muscle myosin acts as a molecular motor only if the regulatory light chain (RLC) is phosphorylated. This subunit can be removed from myosin by a novel method involving the use of trifluoperazine. The motility of RLC-deficient myosin is very slow, but native properties are restored when RLC is rebound. Truncating 6 residues from the COOH terminus of the RLC had no effect on phosphorylated myosin's motor properties, while removal of the last 12 residues reduced velocity by approximately 30%. Very slow movement was observed once 26 residues were deleted, or with myosin containing only the COOH-terminal RLC domain. These two mutants thus mimicked the behavior of RLC-deficient myosin, with the important difference that the mutant myosins were monodisperse when assayed by sedimentation velocity and electron microscopy. The decreased motility therefore cannot be caused by aggregation. A common feature of RLC-deficient myosin and the mutant myosins that moved actin slowly was an increased myosin ATPase compared with dephosphorylated myosin, and a lower actin-activated ATPase than obtained with phosphorylated myosin. These results suggest that the COOH-terminal portion of an intact RLC is involved in interactions that regulate myosin's "on-off" switch, both in terms of completely inhibiting and completely activating the molecule.
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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.