ArticleThe Journal of biological chemistry2013
Kinetic characterization of the ATPase and actin-activated ATPase activities of Acanthamoeba castellanii myosin-2.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 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.
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Who cites it
7 citing papers in PubMed, 10 citations in OpenAlex.
- Structure, regulation, and mechanisms of nonmuscle myosin-2.Cellular and molecular life sciences : CMLS · 2024Review
- Actomyosin Complex.Sub-cellular biochemistry · 2022Article
- CaATP prolongs strong actomyosin binding and promotes futile myosin stroke.Journal of muscle research and cell motility · 2019Article
- Coarse-grained simulations of actomyosin rings point to a nodeless model involving both unipolar and bipolar myosins.Molecular biology of the cell · 2018Article
- Interacting-heads motif has been conserved as a mechanism of myosin II inhibition since before the origin of animals.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Various Themes of Myosin Regulation.Journal of molecular biology · 2016Review
- Kinetic characterization of the sole nonmuscle myosin-2 from the model organism Drosophila melanogaster.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2015Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Phosphorylation of Ser-639 in loop-2 of the catalytic motor domain of the heavy chain of Acanthamoeba castellanii myosin-2 and the phosphomimetic mutation S639D have been shown previously to down-regulate the actin-activated ATPase activity of both the full-length myosin and single-headed subfragment-1 (Liu, X., Lee, D. Y., Cai, S., Yu, S., Shu, S., Levine, R. L., and Korn, E. D. (2013) Proc. Natl. Acad. Sci. U.S.A. 110, E23-E32). In the present study we determined the kinetic constants for each step in the myosin and actomyosin ATPase cycles of recombinant wild-type S1 and S1-S639D. The kinetic parameter predominantly affected by the S639D mutation is the actin-activated release of inorganic phosphate from the acto myosin·ADP·Pi complex, which is the rate-limiting step in the steady-state actomyosin ATPase cycle. As consequence of this change, the duty ratio of this conventional myosin decreases. We speculate on the effect of Ser-639 phosphorylation on the processive behavior of myosin-2 filaments.
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