ReviewJournal of muscle research and cell motility2001
Regulation of nonmuscle myosins by heavy chain phosphorylation.
Review in Journal of muscle research and cell motility, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 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
9 citing papers in PubMed, 36 citations in OpenAlex.
- Article
- Calcium-dependent phosphorylation alters class XIVa myosin function in the protozoan parasite Toxoplasma gondii.Molecular biology of the cell · 2014Article
- Non-muscle myosin II regulates neuronal actin dynamics by interacting with guanine nucleotide exchange factors.PloS one · 2014Article
- Myosin heavy chain kinases play essential roles in Ca2+, but not cAMP, chemotaxis and the natural aggregation of Dictyostelium discoideum.Journal of cell science · 2012Article
- A small-molecule inhibitor of T. gondii motility induces the posttranslational modification of myosin light chain-1 and inhibits myosin motor activity.PLoS pathogens · 2010Article
- Caenorhabditis elegans unc-82 encodes a serine/threonine kinase important for myosin filament organization in muscle during growth.Genetics · 2010Article
- Tobacco mosaic virus infection spreads cell to cell as intact replication complexes.Proceedings of the National Academy of Sciences of the United States of America · 2004Article
- Novel myosin heavy chain kinase involved in disassembly of myosin II filaments and efficient cleavage in mitotic dictyostelium cells.Molecular biology of the cell · 2002Article
- Signaling pathways regulating Dictyostelium myosin II.Journal of muscle research and cell motility · 2002Review
Corrections and comments
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Authors and funding
1 author at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Functional activities of many nonmuscle myosin isoforms are (or are postulated to be) regulated by heavy chain phosphorylation. Depending on the myosin isoform, the serine or threonine residues located within the head (myosin I or myosin VI) or within the C-terminal tail domains (myosin II or myosin V) can be phosphorylated by more or less specific endogenous kinases. In some isoforms phosphorylation can occur both in the head and tail domains, as it has been found for myosin III. There are also isoforms that can be regulated both by the heavy and regulatory light chain phosphorylation, as for the example myosin II from slide mold Dictyostelium discoideum. The goal of this review was to describe recent findings on regulation of myosin I, myosin II, myosin III, myosin V and myosin VI isoforms by their heavy chain phosphorylation including the short charcteristics of the relevant kinases. The biological aspects of the phosphorylation are also discussed.
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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.