ArticleThe Journal of cell biology1990
Calmodulin dissociation regulates brush border myosin I (110-kD-calmodulin) mechanochemical activity in vitro.
Article in The Journal of cell biology, 1990. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.
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Who cites it
60 citing papers in PubMed, 187 citations in OpenAlex.
- MYO1B in human disease: an actin-based motor linking membrane trafficking to oncogenic signaling, metastasis, and vascular aging.Frontiers in oncology · 2026Review
- Myosin-1C differentially displaces tropomyosin isoforms altering their inhibition of motility.The Journal of biological chemistry · 2024Article
- Calmodulin: a highly conserved and ubiquitous CaProceedings of the Japan Academy. Series B, Physical and biological sciences · 2024Review
- Pathophysiology of human hearing loss associated with variants in myosins.Frontiers in physiology · 2024Review
- Review
- Discovery of ultrafast myosin, its amino acid sequence, and structural features.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Effects of Mutations in the Phenamacril-Binding Site ofACS omega · 2020Article
- Human myosin 1e tail but not motor domain replaces fission yeast Myo1 domains to support myosin-I function during endocytosis.Experimental cell research · 2019Article
- Tropomyosin isoforms bias actin track selection by vertebrate myosin Va.Molecular biology of the cell · 2016Article
- Myosin-I molecular motors at a glance.Journal of cell science · 2016Review
- Various Themes of Myosin Regulation.Journal of molecular biology · 2016Review
- Regulation of nonmuscle myosin II by tropomyosin.Biochemistry · 2014Article
- Calcium inhibition of ribonuclease H1 two-metal ion catalysis.Journal of the American Chemical Society · 2014Article
- Myosin light chains: Teaching old dogs new tricks.Bioarchitecture · 2014Review
- Fission yeast tropomyosin specifies directed transport of myosin-V along actin cables.Molecular biology of the cell · 2014Article
- Regulation and control of myosin-I by the motor and light chain-binding domains.Trends in cell biology · 2013Review
- Calcium regulation of myosin-I tension sensing.Biophysical journal · 2012Article
- Leveraging the membrane - cytoskeleton interface with myosin-1.Trends in cell biology · 2010Review
- Human deafness mutation E385D disrupts the mechanochemical coupling and subcellular targeting of myosin-1a.Biophysical journal · 2008Article
- Calcium regulation of calmodulin binding to and dissociation from the myo1c regulatory domain.Biochemistry · 2007Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
110-kD-calmodulin, when immobilized on nitrocellulose-coated coverslips, translocates actin filaments at a maximal rate of 0.07-0.1 micron/s at 37 degrees C. Actin activates MgATPase activity greater than 40-fold, with a Km of 40 microM and Vmax of 0.86 s-1 (323 nmol/min/mg). The rate of motility mediated by 110-kD-calmodulin is dependent on temperature and concentration of ATP, but independent of time, actin filament length, amount of enzyme, or ionic strength. Tropomyosin inhibits actin binding by 110-kD-calmodulin in MgATP and inhibits motility. Micromolar calcium slightly increases the rate of motility and increases the actin-activated MgATP hydrolysis of the intact complex. In 0.1 mM or higher calcium, motility ceases and actin-dependent MgATPase activity remains at a low rate not activated by increasing actin concentration. Correlated with these inhibitions of activity, a subset of calmodulin is dissociated from the complex. To determine if calmodulin loss is the cause of calcium inhibition, we assayed the ability of calmodulin to rescue the calcium-inactivated enzyme. Readdition of calmodulin to the nitrocellulose-bound, calcium-inactivated enzyme completely restores motility. Addition of calmodulin also restores actin activation to MgATPase activity in high calcium, but does not affect the activity of the enzyme in EGTA. These results demonstrate that in vitro 110-kD-calmodulin functions as a calcium-sensitive mechanoenzyme, a vertebrate myosin I. The properties of this enzyme suggest that despite unique structure and regulation, myosins I and II share a molecular mechanism of motility.
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