ArticleThe Journal of biological chemistry1993
Reversal of caldesmon binding to myosin with calcium-calmodulin or by phosphorylating caldesmon.
Article in The Journal of biological chemistry, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
11 citing papers in PubMed, 27 citations in OpenAlex.
- Article
- Mechanisms of Vascular Smooth Muscle Contraction and the Basis for Pharmacologic Treatment of Smooth Muscle Disorders.Pharmacological reviews · 2016Review
- The role of caldesmon and its phosphorylation by ERK on the binding force of unphosphorylated myosin to actin.Biochimica et biophysica acta · 2014Article
- Calcium-dependent regulation of interactions of caldesmon with calcium-binding proteins found in growth cones of chick forebrain neurons.Cellular and molecular neurobiology · 2001Article
- Article
- Location and functional characterization of myosin contact sites in smooth muscle caldesmon.The Biochemical journal · 1997Article
- Both N-terminal myosin-binding and C-terminal actin-binding sites on smooth muscle caldesmon are required for caldesmon-mediated inhibition of actin filament velocity.Proceedings of the National Academy of Sciences of the United States of America · 1997Article
- Location of smooth-muscle myosin and tropomyosin binding sites in the C-terminal 288 residues of human caldesmon.The Biochemical journal · 1995Article
- Flexation of caldesmon: effect of conformation on the properties of caldesmon.Journal of muscle research and cell motility · 1995Article
- Phosphorylation of caldesmon by smooth-muscle casein kinase II.Journal of muscle research and cell motility · 1994Article
- Calmodulin and the regulation of smooth muscle contraction.Molecular and cellular biochemistry · 1994Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Caldesmon, an actin-binding protein from smooth muscle and non-muscle cells, has previously been shown to bind stoichiometrically to smooth muscle myosin in an ATP-dependent manner. We now show quantitatively the effects of Ca(2+)-calmodulin and phosphorylation on the binding of caldesmon to myosin. Ca(2+)-calmodulin reduces the binding of caldesmon to myosin with the same effectiveness as it does the binding of caldesmon to actin. However, Ca(2+)-calmodulin is ineffective in antagonizing the binding of the purified myosin-binding region of caldesmon to myosin. These and other results suggest that Ca(2+)-calmodulin binding to the COOH-terminal region of caldesmon is responsible for reversal of binding to myosin. Phosphorylation of the NH2-terminal region of caldesmon by the co-purifying kinase, calmodulin-dependent protein kinase II, weakens but does not eliminate the binding of caldesmon to smooth muscle myosin. Finally, phosphorylation of smooth muscle myosin by smooth muscle myosin light chain kinase has no effect on the binding of caldesmon to myosin. Since Ca(2+)-calmodulin and phosphorylation of caldesmon weaken the binding of caldesmon to both actin and myosin, these events may be coordinately regulated.
Indexed as
Identifiers
8325900PMC1289261W2132347213What OpenQuestion holds
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.