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http://purl.uniprot.org/citations/6452632http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/6452632http://www.w3.org/2000/01/rdf-schema#comment"Dictyostelium myosin is composed of two heavy chains and two pairs of light chains in a 1:1:1 stoichiometry. Myosin purified from amoebae grown in medium containing [32P]phosphate had two of the subunits labeled (0.2-0.3 mol of phosphate per mol of 210,000-dalton heavy chains and approximately 0.1 mol of phosphate per mol of 18,000-dalton light chain). Kinase activities specific for the 210,000-dalton and for the 18,000-dalton subunits have been identified in extracts of Dictyostelium amoebae, and the heavy chain kinase has been purified 50-fold. This kinase phosphorylated Dictyostelium myosin to a maximum of 0.5-1.0 mol of phosphate per mol of heavy chain. Heavy chain phosphate, but not light chain phosphate, can be removed with bacterial alkaline phosphatase. Actin-activated myosin ATPase increased 80% when phosphorylated myosin was dephosphorylated to a level of approximately 0.06 mol of phosphate per mol of heavy chain. This effect could be reversed by rephosphorylating the myosin. The ability of myosin to self-assemble into thick filaments was inhibited by heavy chain phosphorylation. For example, in 80-100 mM KCl, only 10-20% of the myosin was assembled into thick filaments when the heavy chains were fully phosphorylated. Removal of the heavy chain phosphate resulted in 70-90% thick filament formation. This effect on self-assembly could be reversed by rephosphorylating the dephosphorylated myosin. These findings suggest that heavy chain phosphorylation may regulate cell contractile events by altering the state of myosin assembly."xsd:string
http://purl.uniprot.org/citations/6452632http://purl.org/dc/terms/identifier"doi:10.1073/pnas.77.12.7292"xsd:string
http://purl.uniprot.org/citations/6452632http://purl.uniprot.org/core/author"Spudich J.A."xsd:string
http://purl.uniprot.org/citations/6452632http://purl.uniprot.org/core/author"Kuczmarski E.R."xsd:string
http://purl.uniprot.org/citations/6452632http://purl.uniprot.org/core/date"1980"xsd:gYear
http://purl.uniprot.org/citations/6452632http://purl.uniprot.org/core/name"Proc Natl Acad Sci U S A"xsd:string
http://purl.uniprot.org/citations/6452632http://purl.uniprot.org/core/pages"7292-7296"xsd:string
http://purl.uniprot.org/citations/6452632http://purl.uniprot.org/core/title"Regulation of myosin self-assembly: phosphorylation of Dictyostelium heavy chain inhibits formation of thick filaments."xsd:string
http://purl.uniprot.org/citations/6452632http://purl.uniprot.org/core/volume"77"xsd:string
http://purl.uniprot.org/citations/6452632http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/6452632
http://purl.uniprot.org/citations/6452632http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/6452632
http://purl.uniprot.org/uniprot/#_P42527-mappedCitation-6452632http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/6452632
http://purl.uniprot.org/uniprot/#_P08799-mappedCitation-6452632http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/6452632
http://purl.uniprot.org/uniprot/#_P25323-mappedCitation-6452632http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/6452632
http://purl.uniprot.org/uniprot/P08799http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/6452632
http://purl.uniprot.org/uniprot/P25323http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/6452632
http://purl.uniprot.org/uniprot/P42527http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/6452632