ArticleProceedings of the National Academy of Sciences of the United States of America1997
Slow cycling of unphosphorylated myosin is inhibited by calponin, thus keeping smooth muscle relaxed.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 53 citations in OpenAlex.
- UNC-87 isoforms, Caenorhabditis elegans calponin-related proteins, interact with both actin and myosin and regulate actomyosin contractility.Molecular biology of the cell · 2015Article
- Cytoskeletal reorganization evoked by Rho-associated kinase- and protein kinase C-catalyzed phosphorylation of cofilin and heat shock protein 27, respectively, contributes to myogenic constriction of rat cerebral arteries.The Journal of biological chemistry · 2014Article
- Unphosphorylated calponin enhances the binding force of unphosphorylated myosin to actin.Biochimica et biophysica acta · 2013Article
- Molluscan smooth catch muscle contains calponin but not caldesmon.Journal of muscle research and cell motility · 2013Article
- New insights into myosin phosphorylation during cyclic nucleotide-mediated smooth muscle relaxation.Journal of muscle research and cell motility · 2012Article
- The effect of L-arginine on bladder dysfunction following ovariectomy in a rabbit model.International urogynecology journal · 2011Article
- Inducible knockout mutagenesis reveals compensatory mechanisms elicited by constitutive BK channel deficiency in overactive murine bladder.The FEBS journal · 2009Article
- Ontogenesis of myosin light chain phosphorylation in guinea pig tracheal smooth muscle.Pediatric pulmonology · 2005Article
- Ontogenesis of myosin light chain kinase mRNA and protein content in guinea pig tracheal smooth muscle.Pediatric pulmonology · 2004Article
- Essential role of rho kinase in the Ca2+ sensitization of prostaglandin F(2alpha)-induced contraction of rabbit aortae.The Journal of physiology · 2003Article
- Regulatory and essential light chains of myosin rotate equally during contraction of skeletal muscle.Biophysical journal · 2002Article
- Calponin is required for agonist-induced signal transduction--evidence from an antisense approach in ferret smooth muscle.The Journal of physiology · 2001Article
- The myosin cross-bridge cycle and its control by twitchin phosphorylation in catch muscle.Biophysical journal · 2001Article
- Contractile properties and proteins of smooth muscles of a calponin knockout mouse.The Journal of physiology · 2000Article
- A tribute to Fredric Stewart Fay: June 5, 1943 - March 18, 1997.Biophysical journal · 1998Article
- Cytoskeletal targeting of calponin in differentiated, contractile smooth muscle cells of the ferret.The Journal of physiology · 1998Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A key unanswered question in smooth muscle biology is whether phosphorylation of the myosin regulatory light chain (RLC) is sufficient for regulation of contraction, or if thin-filament-based regulatory systems also contribute to this process. To address this issue, the endogenous RLC was extracted from single smooth muscle cells and replaced with either a thiophosphorylated RLC or a mutant RLC (T18A/S19A) that cannot be phosphorylated by myosin light chain kinase. The actin-binding protein calponin was also extracted. Following photolysis of caged ATP, cells without calponin that contained a nonphosphorylatable RLC shortened at 30% of the velocity and produced 65% of the isometric force of cells reconstituted with the thiophosphorylated RLC. The contraction of cells reconstituted with nonphosphorylatable RLC was, however, specifically suppressed in cells that contained calponin. These results indicate that calponin is required to maintain cells in a relaxed state, and that in the absence of this inhibition, dephosphorylated cross-bridges can slowly cycle and generate force. These findings thus provide a possible framework for understanding the development of latch contraction, a widely studied but poorly understood feature of smooth muscle.
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