| http://purl.uniprot.org/citations/3032987 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/3032987 | http://www.w3.org/2000/01/rdf-schema#comment | "We have partially purified myosin light chain kinase (MLCK) and myosin light chain phosphatase (MLCP) from Dictyostelium discoideum. MLCK was purified 4,700-fold with a yield of approximately 1 mg from 350 g of cells. The enzyme is very acidic as suggested by its tight binding to DEAE. Dictyostelium MLCK has an apparent native molecular mass on HPLC G3000SW of approximately 30,000 D. Mg2+ is required for enzyme activity. Ca2+ inhibits activity and this inhibition is not relieved by calmodulin. cAMP or cGMP have no effect on enzyme activity. Dictyostelium MLCK is very specific for the 18,000-D light chain of Dictyostelium myosin and does not phosphorylate the light chain of several other myosins tested. Myosin purified from log-phase amebas of Dictyostelium has approximately 0.3 mol Pi/mol 18,000-D light chain as assayed by glycerol-urea gel electrophoresis. Dictyostelium MLCK can phosphorylate this myosin to a stoichiometry approaching 1 mol Pi/mol 18,000-D light chain. MLCP, which was partially purified, selectively removes phosphate from the 18,000-D light chain but not from the heavy chain of Dictyostelium myosin. Phosphatase-treated Dictyostelium myosin has less than or equal to 0.01 mol Pi/mol 18,000-D light chain. Phosphatase-treated myosin could be rephosphorylated to greater than or equal to 0.96 mol Pi/mol 18,000-D light chain by incubation with MLCK and ATP. We found myosin thick filament assembly to be independent of the extent of 18,000-D light-chain phosphorylation when measured as a function of ionic strength. However, actin-activated Mg2+-ATPase activity of Dictyostelium myosin was found to be directly related to the extent of phosphorylation of the 18,000-D light chain. MLCK-treated myosin moved in an in vitro motility assay (Sheetz, M. P., and J. A. Spudich, 1983, Nature (Lond.), 305:31-35) at approximately 1.4 micron/s whereas phosphatase-treated myosin moved only slowly or not at all. The effects of phosphatase treatment on the movement were fully reversed by subsequent treatment with MLCK."xsd:string |
| http://purl.uniprot.org/citations/3032987 | http://purl.org/dc/terms/identifier | "doi:10.1083/jcb.104.5.1309"xsd:string |
| http://purl.uniprot.org/citations/3032987 | http://purl.uniprot.org/core/author | "Spudich J.A."xsd:string |
| http://purl.uniprot.org/citations/3032987 | http://purl.uniprot.org/core/author | "Downs S.M."xsd:string |
| http://purl.uniprot.org/citations/3032987 | http://purl.uniprot.org/core/author | "Griffith L.M."xsd:string |
| http://purl.uniprot.org/citations/3032987 | http://purl.uniprot.org/core/date | "1987"xsd:gYear |
| http://purl.uniprot.org/citations/3032987 | http://purl.uniprot.org/core/name | "J Cell Biol"xsd:string |
| http://purl.uniprot.org/citations/3032987 | http://purl.uniprot.org/core/pages | "1309-1323"xsd:string |
| http://purl.uniprot.org/citations/3032987 | http://purl.uniprot.org/core/title | "Myosin light chain kinase and myosin light chain phosphatase from Dictyostelium: effects of reversible phosphorylation on myosin structure and function."xsd:string |
| http://purl.uniprot.org/citations/3032987 | http://purl.uniprot.org/core/volume | "104"xsd:string |
| http://purl.uniprot.org/citations/3032987 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/3032987 |
| http://purl.uniprot.org/citations/3032987 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/3032987 |
| http://purl.uniprot.org/uniprot/P25323#attribution-A83C7FC4BC99F5118B44389580A798DC | http://purl.uniprot.org/core/source | http://purl.uniprot.org/citations/3032987 |
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| http://purl.uniprot.org/uniprot/P25323 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/3032987 |