FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W1976750469> ?p ?o ?g. }

• W1976750469 endingPage "25878" @default.
• W1976750469 startingPage "25872" @default.
• W1976750469 abstract "The α and β subunits of casein kinase II are dramatically phosphorylated in cells that are arrested in mitosis (Litchfield, D. W., Lüscher, B., Lozeman, F. J., Eisenman, R. N., and Krebs, E. G.(1992) J. Biol. Chem. 267, 13943-13951). Comparative phosphopeptide mapping experiments indicated that the mitotic phosphorylation sites on the α subunit of casein kinase II can be phosphorylated in vitro by p34cdc2. In the present study, we have demonstrated that a glutathione S-transferase fusion protein encoding the C-terminal 126 amino acids of the α subunit is phosphorylated by p34cdc2 at the same sites as intact casein kinase II, indicating that the mitotic phosphorylation sites are localized within the C-terminal domain of α. Four residues within this domain, Thr-344, Thr-360, Ser-362, and Ser-370, conform to the minimal consensus sequence for p34cdc2 phosphorylation. Synthetic peptides corresponding to regions of α that contain each of these residues are phosphorylated by p34cdc2 at these sites. Furthermore, alterations in the phosphorylation of the glutathione S-transferase proteins encoding the C-terminal domain of α are observed when any of the four residues are mutated to alanine. When all four residues are mutated to alanine, the fusion protein is no longer phosphorylated by p34cdc2 at any of the sites that are phosphorylated in mitotic cells. These results indicate that Thr-344, Thr-360, Ser-362, and Ser-370 are the sites on the α subunit of casein kinase II that are phosphorylated in mitotic cells. The α and β subunits of casein kinase II are dramatically phosphorylated in cells that are arrested in mitosis (Litchfield, D. W., Lüscher, B., Lozeman, F. J., Eisenman, R. N., and Krebs, E. G.(1992) J. Biol. Chem. 267, 13943-13951). Comparative phosphopeptide mapping experiments indicated that the mitotic phosphorylation sites on the α subunit of casein kinase II can be phosphorylated in vitro by p34cdc2. In the present study, we have demonstrated that a glutathione S-transferase fusion protein encoding the C-terminal 126 amino acids of the α subunit is phosphorylated by p34cdc2 at the same sites as intact casein kinase II, indicating that the mitotic phosphorylation sites are localized within the C-terminal domain of α. Four residues within this domain, Thr-344, Thr-360, Ser-362, and Ser-370, conform to the minimal consensus sequence for p34cdc2 phosphorylation. Synthetic peptides corresponding to regions of α that contain each of these residues are phosphorylated by p34cdc2 at these sites. Furthermore, alterations in the phosphorylation of the glutathione S-transferase proteins encoding the C-terminal domain of α are observed when any of the four residues are mutated to alanine. When all four residues are mutated to alanine, the fusion protein is no longer phosphorylated by p34cdc2 at any of the sites that are phosphorylated in mitotic cells. These results indicate that Thr-344, Thr-360, Ser-362, and Ser-370 are the sites on the α subunit of casein kinase II that are phosphorylated in mitotic cells." @default.
• W1976750469 created "2016-06-24" @default.
• W1976750469 creator A5001153640 @default.
• W1976750469 creator A5044899640 @default.
• W1976750469 creator A5082963457 @default.
• W1976750469 creator A5086809539 @default.
• W1976750469 date "1995-10-01" @default.
• W1976750469 modified "2023-10-14" @default.
• W1976750469 title "Phosphorylation of Casein Kinase II by p34cdc2" @default.
• W1976750469 cites W11746033 @default.
• W1976750469 cites W1482405769 @default.
• W1976750469 cites W1505972278 @default.
• W1976750469 cites W1528493806 @default.
• W1976750469 cites W1530475739 @default.
• W1976750469 cites W1531747712 @default.
• W1976750469 cites W1577781729 @default.
• W1976750469 cites W1594985705 @default.
• W1976750469 cites W1599938904 @default.
• W1976750469 cites W1607643143 @default.
• W1976750469 cites W1782290346 @default.
• W1976750469 cites W1783266809 @default.
• W1976750469 cites W1805369505 @default.
• W1976750469 cites W1846585173 @default.
• W1976750469 cites W1896934695 @default.
• W1976750469 cites W1898229949 @default.
• W1976750469 cites W1952982568 @default.
• W1976750469 cites W1970575648 @default.
• W1976750469 cites W1979629909 @default.
• W1976750469 cites W2024973560 @default.
• W1976750469 cites W2036931150 @default.
• W1976750469 cites W2038143768 @default.
• W1976750469 cites W2039905204 @default.
• W1976750469 cites W2044145281 @default.
• W1976750469 cites W2044336308 @default.
• W1976750469 cites W2048875557 @default.
• W1976750469 cites W2049355608 @default.
• W1976750469 cites W2057230968 @default.
• W1976750469 cites W2058022253 @default.
• W1976750469 cites W2059155490 @default.
• W1976750469 cites W2062707142 @default.
• W1976750469 cites W2063797024 @default.
• W1976750469 cites W2068446924 @default.
• W1976750469 cites W2085652293 @default.
• W1976750469 cites W2087656195 @default.
• W1976750469 cites W2100837269 @default.
• W1976750469 cites W2124030177 @default.
• W1976750469 cites W2137249911 @default.
• W1976750469 cites W2138270253 @default.
• W1976750469 cites W2166270104 @default.
• W1976750469 cites W2172197731 @default.
• W1976750469 cites W2175640000 @default.
• W1976750469 cites W2235427389 @default.
• W1976750469 cites W2270599862 @default.
• W1976750469 cites W301681196 @default.
• W1976750469 cites W3022312892 @default.
• W1976750469 cites W4253622855 @default.
• W1976750469 cites W4293247451 @default.
• W1976750469 cites W99328058 @default.
• W1976750469 doi "https://doi.org/10.1074/jbc.270.43.25872" @default.
• W1976750469 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/7592773" @default.
• W1976750469 hasPublicationYear "1995" @default.
• W1976750469 type Work @default.
• W1976750469 sameAs 1976750469 @default.
• W1976750469 citedByCount "79" @default.
• W1976750469 countsByYear W19767504692012 @default.
• W1976750469 countsByYear W19767504692013 @default.
• W1976750469 countsByYear W19767504692014 @default.
• W1976750469 countsByYear W19767504692015 @default.
• W1976750469 countsByYear W19767504692017 @default.
• W1976750469 countsByYear W19767504692018 @default.
• W1976750469 countsByYear W19767504692019 @default.
• W1976750469 countsByYear W19767504692021 @default.
• W1976750469 countsByYear W19767504692022 @default.
• W1976750469 countsByYear W19767504692023 @default.
• W1976750469 crossrefType "journal-article" @default.
• W1976750469 hasAuthorship W1976750469A5001153640 @default.
• W1976750469 hasAuthorship W1976750469A5044899640 @default.
• W1976750469 hasAuthorship W1976750469A5082963457 @default.
• W1976750469 hasAuthorship W1976750469A5086809539 @default.
• W1976750469 hasBestOaLocation W19767504691 @default.
• W1976750469 hasConcept C104292427 @default.
• W1976750469 hasConcept C104317684 @default.
• W1976750469 hasConcept C11960822 @default.
• W1976750469 hasConcept C143910341 @default.
• W1976750469 hasConcept C153911025 @default.
• W1976750469 hasConcept C160110348 @default.
• W1976750469 hasConcept C184235292 @default.
• W1976750469 hasConcept C185592680 @default.
• W1976750469 hasConcept C205744416 @default.
• W1976750469 hasConcept C2779933727 @default.
• W1976750469 hasConcept C55493867 @default.
• W1976750469 hasConcept C82495950 @default.
• W1976750469 hasConcept C86803240 @default.
• W1976750469 hasConcept C87325107 @default.
• W1976750469 hasConcept C93304396 @default.
• W1976750469 hasConcept C95444343 @default.
• W1976750469 hasConcept C97029542 @default.
• W1976750469 hasConceptScore W1976750469C104292427 @default.

• next