2014
Regulation of Protein Phosphatase 1I by Cdc25C-associated Kinase 1 (C-TAK1) and PFTAIRE Protein Kinase*
Platholi J, Federman A, Detert JA, Heerdt P, Hemmings HC. Regulation of Protein Phosphatase 1I by Cdc25C-associated Kinase 1 (C-TAK1) and PFTAIRE Protein Kinase*. Journal Of Biological Chemistry 2014, 289: 23893-23900. PMID: 25028520, PMCID: PMC4156073, DOI: 10.1074/jbc.m114.557744.Peer-Reviewed Original ResearchConceptsProtein phosphatase 1IC-TAK1Protein kinaseKinase 1GSK-3Protein phosphatase 1Phosphatase activityPP-1cThr-72Multisite phosphorylationActivating residuesPhosphatase 1Regulatory subunitSer-86Ser-71Subsequent phosphorylationMajor endogenous formsInhibitor 2PhosphorylationKinaseCdc25CEndogenous formPFTK1ResiduesActivation
1997
Characterization of the interaction between DARPP-32 and protein phosphatase 1 (PP-1): DARPP-32 peptides antagonize the interaction of PP-1 with binding proteins
Kwon Y, Huang H, Desdouits F, Girault J, Greengard P, Nairn A. Characterization of the interaction between DARPP-32 and protein phosphatase 1 (PP-1): DARPP-32 peptides antagonize the interaction of PP-1 with binding proteins. Proceedings Of The National Academy Of Sciences Of The United States Of America 1997, 94: 3536-3541. PMID: 9108011, PMCID: PMC20474, DOI: 10.1073/pnas.94.8.3536.Peer-Reviewed Original ResearchConceptsPP-1cPP-1C.PP-1DARPP-32Inhibitor 2Protein phosphatase 1Amino acid sequence analysisAmino acid residuesNH2-terminal regionAcid sequence analysisPhosphoinhibitor-1Threonine residuesPhosphatase 1Inhibitor-1Catalytic subunitCalyculin AOkadaic acidInhibitor proteinActive siteAcid residuesSequence analysisProteinEnzyme activityMotifResidues
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