FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2026987638> ?p ?o ?g. }

• W2026987638 endingPage "3549" @default.
• W2026987638 startingPage "3544" @default.
• W2026987638 abstract "Serine 657 in protein kinase C-α (PKCα) is a site of phosphorylation on expression of the recombinant protein in mammalian cells. To define the function of this phosphorylation, PKCα species with mutations of this site were investigated. The alanine mutant, S657A PKCα, displayed slow phosphate accumulation in pulse-chase experiments, indicating a rate-limiting role in the initial phase of phosphorylation. Consistent with this, the aspartic acid mutant, S657D PKCα, showed an increased rate of phosphate accumulation. Both the S657D and S657A PKCα mutants were slow to accumulate as fully phosphorylated forms during a second phase of phosphorylation. This latter property is shown to correlate with an increased phosphatase sensitivity and decreased protein kinase activity for these two PKCα mutants. It is further shown that once fully phosphorylated, the S657D PKCα mutant displays WT PKCα properties with respect to thermal stability and phosphatase sensitivity in vitro and in vivo; in contrast, the S657A PKCα mutant remains sensitive. The properties of the Ser-657 site PKCα mutants define functional roles for this phosphorylation in both the accumulation of phosphate on PKCα as well as in its agonist-induced dephosphorylation. These results are discussed in the context of a working model of PKCα behavior, providing insight into the workings of other kinases with equivalent sites of phosphorylation. Serine 657 in protein kinase C-α (PKCα) is a site of phosphorylation on expression of the recombinant protein in mammalian cells. To define the function of this phosphorylation, PKCα species with mutations of this site were investigated. The alanine mutant, S657A PKCα, displayed slow phosphate accumulation in pulse-chase experiments, indicating a rate-limiting role in the initial phase of phosphorylation. Consistent with this, the aspartic acid mutant, S657D PKCα, showed an increased rate of phosphate accumulation. Both the S657D and S657A PKCα mutants were slow to accumulate as fully phosphorylated forms during a second phase of phosphorylation. This latter property is shown to correlate with an increased phosphatase sensitivity and decreased protein kinase activity for these two PKCα mutants. It is further shown that once fully phosphorylated, the S657D PKCα mutant displays WT PKCα properties with respect to thermal stability and phosphatase sensitivity in vitro and in vivo; in contrast, the S657A PKCα mutant remains sensitive. The properties of the Ser-657 site PKCα mutants define functional roles for this phosphorylation in both the accumulation of phosphate on PKCα as well as in its agonist-induced dephosphorylation. These results are discussed in the context of a working model of PKCα behavior, providing insight into the workings of other kinases with equivalent sites of phosphorylation." @default.
• W2026987638 created "2016-06-24" @default.
• W2026987638 creator A5000996602 @default.
• W2026987638 creator A5083509118 @default.
• W2026987638 date "1997-02-01" @default.
• W2026987638 modified "2023-10-18" @default.
• W2026987638 title "Phosphorylation of Protein Kinase C-α on Serine 657 Controls the Accumulation of Active Enzyme and Contributes to Its Phosphatase-resistant State" @default.
• W2026987638 cites W1557726768 @default.
• W2026987638 cites W1568928604 @default.
• W2026987638 cites W1585385265 @default.
• W2026987638 cites W1596486131 @default.
• W2026987638 cites W1844603538 @default.
• W2026987638 cites W1965727075 @default.
• W2026987638 cites W1979420700 @default.
• W2026987638 cites W1983138147 @default.
• W2026987638 cites W1994631727 @default.
• W2026987638 cites W2009856702 @default.
• W2026987638 cites W2030347963 @default.
• W2026987638 cites W2050006947 @default.
• W2026987638 cites W2054246670 @default.
• W2026987638 cites W2057069307 @default.
• W2026987638 cites W2058138221 @default.
• W2026987638 cites W2067405360 @default.
• W2026987638 cites W2068502127 @default.
• W2026987638 cites W2088072731 @default.
• W2026987638 cites W2089040137 @default.
• W2026987638 cites W2089475281 @default.
• W2026987638 cites W2091455173 @default.
• W2026987638 cites W2100837269 @default.
• W2026987638 cites W2141524439 @default.
• W2026987638 cites W2170134847 @default.
• W2026987638 cites W2240068561 @default.
• W2026987638 doi "https://doi.org/10.1074/jbc.272.6.3544" @default.
• W2026987638 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/9013603" @default.
• W2026987638 hasPublicationYear "1997" @default.
• W2026987638 type Work @default.
• W2026987638 sameAs 2026987638 @default.
• W2026987638 citedByCount "192" @default.
• W2026987638 countsByYear W20269876382012 @default.
• W2026987638 countsByYear W20269876382013 @default.
• W2026987638 countsByYear W20269876382014 @default.
• W2026987638 countsByYear W20269876382015 @default.
• W2026987638 countsByYear W20269876382016 @default.
• W2026987638 countsByYear W20269876382017 @default.
• W2026987638 countsByYear W20269876382018 @default.
• W2026987638 countsByYear W20269876382019 @default.
• W2026987638 countsByYear W20269876382020 @default.
• W2026987638 countsByYear W20269876382021 @default.
• W2026987638 countsByYear W20269876382022 @default.
• W2026987638 countsByYear W20269876382023 @default.
• W2026987638 crossrefType "journal-article" @default.
• W2026987638 hasAuthorship W2026987638A5000996602 @default.
• W2026987638 hasAuthorship W2026987638A5083509118 @default.
• W2026987638 hasBestOaLocation W20269876381 @default.
• W2026987638 hasConcept C104317684 @default.
• W2026987638 hasConcept C11960822 @default.
• W2026987638 hasConcept C143065580 @default.
• W2026987638 hasConcept C153911025 @default.
• W2026987638 hasConcept C178666793 @default.
• W2026987638 hasConcept C181912034 @default.
• W2026987638 hasConcept C184235292 @default.
• W2026987638 hasConcept C195794163 @default.
• W2026987638 hasConcept C2776414213 @default.
• W2026987638 hasConcept C55493867 @default.
• W2026987638 hasConcept C86803240 @default.
• W2026987638 hasConcept C87325107 @default.
• W2026987638 hasConcept C95444343 @default.
• W2026987638 hasConcept C97029542 @default.
• W2026987638 hasConceptScore W2026987638C104317684 @default.
• W2026987638 hasConceptScore W2026987638C11960822 @default.
• W2026987638 hasConceptScore W2026987638C143065580 @default.
• W2026987638 hasConceptScore W2026987638C153911025 @default.
• W2026987638 hasConceptScore W2026987638C178666793 @default.
• W2026987638 hasConceptScore W2026987638C181912034 @default.
• W2026987638 hasConceptScore W2026987638C184235292 @default.
• W2026987638 hasConceptScore W2026987638C195794163 @default.
• W2026987638 hasConceptScore W2026987638C2776414213 @default.
• W2026987638 hasConceptScore W2026987638C55493867 @default.
• W2026987638 hasConceptScore W2026987638C86803240 @default.
• W2026987638 hasConceptScore W2026987638C87325107 @default.
• W2026987638 hasConceptScore W2026987638C95444343 @default.
• W2026987638 hasConceptScore W2026987638C97029542 @default.
• W2026987638 hasIssue "6" @default.
• W2026987638 hasLocation W20269876381 @default.
• W2026987638 hasOpenAccess W2026987638 @default.
• W2026987638 hasPrimaryLocation W20269876381 @default.
• W2026987638 hasRelatedWork W1883788376 @default.
• W2026987638 hasRelatedWork W1977619913 @default.
• W2026987638 hasRelatedWork W2015932636 @default.
• W2026987638 hasRelatedWork W2026987638 @default.
• W2026987638 hasRelatedWork W2042668741 @default.
• W2026987638 hasRelatedWork W2043717361 @default.
• W2026987638 hasRelatedWork W2086061243 @default.
• W2026987638 hasRelatedWork W2109572947 @default.
• W2026987638 hasRelatedWork W3037320846 @default.
• W2026987638 hasRelatedWork W1966079516 @default.
• W2026987638 hasVolume "272" @default.
• W2026987638 isParatext "false" @default.

• next