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J. Biol. Chem. 281, 4754-4761. Casein Kinase II phosphorylation of the yeast phospholipid synthesis transcription factor Opi1p. 2006

Chang, Y-F. and Carman, G.M.

Notes: Opi1p is a transcriptional repressor that regulates phospholipid synthesis in yeast. Opi1p activity is regulated by protein kinase C (PKC) and cAMP-dependent protein kinase (PKA). This study investigates the role of casein kinase II (CaMK II) in regulation of Opi1p activity. PKC and PKA were used in phosphorylation studies to determine how specific mutations within Opi1p affect phosphorylation. (3536)

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J. Biol. Chem. 280, 26105-26112. Phosphorylation of the yeast choline kinase by protein kinase C. 2005

Choi, M-G., Kurnov, V., Kersting, M.C., Sreenivas, A., and Carman, G.M.

Notes: In this study, the authors investigated the role of Protein Kinase C in the phosphorylation of choline kinase, which is thought to play a role in the generation of human tumors. cAMP-Dependent Protein Kinase, Catalytic Subunit, and Protein Kinase C were used in phosphorylation reactions of pure choline kinase, immunoprecipitated choline kinase and choline kinase synthetic peptides. (3507)

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Mol. Cell. Biol. 24, 6205-6214. Rac1 Inhibits Apoptosis in Human Lymphoma Cells by Stimulating Bad Phosphorylation on Ser-75. 2004

Zhang, B., Zhang, Y., and Shacter, E.

Notes: Researchers used Promega’s cAMP-Dependent Protein Kinase Peptide Inhibitor to demonstrate that BAD kinase is phosphorylated through a cAMP-Dependent Protein Kinase (PKA) dependent pathway in Burkitt’s lymphoma BL-41 cells.  The PepTag® Non-Radioactive cAMP-Dependent Protein Kinase Assay was used to demonstrate PKA activity in BL-41 cell lysates.  In these experiments the researchers added cAMP with and without Promega’s cAMP-Dependent Protein Kinase Peptide Inhibitor (20μM) or Rp-cAMPS (100μM) to 0.2-2ug of BL-41 cell lysate.  Images of gels were depicted in the paper. (3134)

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EMBO J. 19(12), 2946-2957.

Phosphorylation status of the SCR homeodomain determines its functional activity: Essential role for protein phosphatase 2A,B'. 2000

Berry, M. and Gehring, W.

Notes: The Serine-Threonine Phosphatase Assay System was used to monitor dephosphorylation of two phosphopeptides derived from the SCR homeodomain. Dephosphorylation was performed using the catalytic subunit of the PP2A protein. Authors also used pSI for cloning, protein kinase A enzyme, PKA and PKC assays using biotinylated peptides (SignaTECT® Protein Kinase assay systems), anti-β-galactosidase for Drosophila embryo staining, and TNT® Quick Coupled Transcription/Translation systems to produce mutant and wild type protein for gel shifts. (2150)

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J. Biol. Chem. 275, 14360-14366. Protein kinase A associates with cystic fibrosis transmembrane conductance regulator via an interaction with Ezrin 2000

Sun, F., Hug, M.J., Bradbury, N.A., Frizzell, R.A.

Notes: Immunoprecipitates of CFTR become phosphorylated upon addition of a PKA catalytic subunit which is inhibitable by the Protein Kinase A Inhibitor Peptide. The SignaTECT® cAMP-Dependent Protein Kinase Assay System was used to measure PKA activity in immunoprecipitates of the CFTR protein. The activity was almost totally inhibited by the Protein Kinase A Inhibitor Peptide. PKA activity was four times higher with the anti-CFTR antibody precipitates than with a control antibody and addition of cAMP increased the amount of phosphorylation observed in the immunoprecipitates. Immunoprecipitates were prepared from Calu-3 human airway epithelia cells. (0318)

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J. Biol. Chem. 274, 3485-3495. Phosphorylation-dependent inhibition of protein phosphatase-1 by G-substrate. A Purkinje cell substrate of the cyclic GMP-dependent protein kinase. 1999

Hall, K.U., Collins, S.P., Gamm, D.M., Massa, E., DePaoli Roach, A.A., Uhler, M.D.

Notes: The authors used cGMP-Dependent Protein Kinase (PKG) to phosphorylate their particular substrate. They also used cAMP-Dependent Protein Kinase, Catalytic Subunit (PKA) to phosphorylate human recombinant DARPP-32 (dopamine- and adenosine 3´:5´-monophosphate-regulated phosphoprotein-32,000). (1095)

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Am. J. Physiol. 274, L305-L312. Fluoride stimulates cystic fibrosis transmembrane conductance regulator Cl- channel activity. 1998

Berger, H.A., Travis, S.M. and Welsh, M.J.

Notes: The authors used purified cAMP-dependent Protein Kinase (PKA) to in vitro phosphorylate and activate CFTR. (2237)

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J. Biol. Chem. 273, 5670-5677. Phosphorylation of inositol 1,4,5-trisphosphate receptors by cAMP-dependent protein kinase: Type I, II and III receptors are differentially susceptible to phophorylation and are phosphorylated in intact cells. 1998

Wojcikiewicz, R.J.H., Luo, S.G.

Notes: The cAMP-dependent Protein Kinase, Catalytic Subunit (PKA) was used for in vitro phosphorylation of isolated, purified InsP3 receptors. The cAMP-dependent Protein Kinase, Catalytic Subunit (PKA)  was also used to asses the ability of isolated InsP3 receptors to be 32P-phosphorylated. The lack of 32P-phosphorylation was related to the native phosphorylation state of the isolated receptor. (0147)

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Am. J. Physiol. 274, F175-F181. Role of the NH2 terminus of the cloned renal K+ channel, ROMK1, in arachidonic acid-mediated inhibition. 1998

Macica, C.M., Yang, Y., Lerea, K., Hebert, S.C. , Wang, W.

Notes: The authors used the cAMP-Dependent Protein Kinase, Catalytic Subunit in their studies on Xenopus oocytes. (0763)

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EMBO J. 16, 2420-2430. A single serine residue at position 375 of VP16 is critical for complex assembly with Oct-1 and HCF and is a target of phosphorylation by casein kinase II. 1997

O'Reilly, D., Hanscombe, O., O'Hare, P.

Notes: The cAMP-dependent Protein Kinase (PKA) was used to in vitro phosphorylate VP16. Details are provided for the reaction buffers for each reaction. (0564)

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J. Biol. Chem. 272, 25617-25622.. Covalent modification of the regulatory domain irreversibly stimulates cystic fibrosis transmembrane conductance regulator 1997

Cotten, J. F. , Welsh, M. J.

Notes: The cAMP-Dependent Protein Kinase, Catalytic Subunit (PKA) was used to activate the CFTR from excised, inside-out membranes from transfected HeLa cells. A lot of detail for the kinase reaction is provided. (1280)

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J. Biol. Chem. 272, 14037-14040. Cystic fibrosis transmembrane conductance regulator inverts protein kinase A-mediated regulation of epithelial sodium channel single channel kinetics. 1997

Stutts, M.J., Rossier, B.C., Boucher, R.C.

Notes: cAMP-Dependent Protein Kinase (PKA) studies were performed with membrane patches of NIH3T3 cells transfected with several transmembrane proteins. (0306)

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EMBO J. 16, 35-43.. Ezrin is a cyclic AMP-dependent protein kinase anchoring protein. 1997

Dransfield, D. T. , Bradford, A. J. , Smith, J. , Martin, M. , Roy, C. , Mangeat, P. H. , Goldenring, J. R.

Notes: The catalytic subunit of cAMP-dependent Protein Kinase (PKA) was used to in vitro phosphorylate the bacterially-expressed, purified type II A-kinase regulatory subunit. (1249)

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J. Biol. Chem. 272, 28133-28141. Function of the R domain in the cystic fibrosis transmembrane conductance regulator chloride channel 1997

Ma, J., Zhao, J., Drumm, M.L., Xie, J., Davis, P.B.

Notes: The cAMP-dependent Protein Kinase was used to in vitro phosphorylate the R domain in a synthetic lipid bilayer. Many details of the reconstitution of the channel are given. The Protein Phosphatase 2A was used to be sure that the R domain mutate that did not work when phosphorylated worked equally as poorly without the phosphate. (0758)

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Am. J. Physiol. 273, L913-L920. Glycosylation differences between a cystic fibrosis and rescued airway cell line are not CFTR dependent. 1997

Jiang, X., Hill, W.G., Pilewski, J.M., Weisz, O.A.

Notes: The authors immunoprecipitated CFTR and performed an in vitro kinase reaction using the cAMP-Dependent Protein Kinase, Catalytic Subunit (PKA) and [γ32P] ATP. (0980)

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J. Biol. Chem. 272, 26219-26225. Interaction of phosphorylated tryptophan hydroxylase with 14-3-3 proteins 1997

Banik, U., Wang, G.A., Wagner, P.D., Kaufman, S.

Notes: In this paper, rabbit brain tryptophan hydroxylase was phosphorylated in vitro using 32P and cAMP-Dependent Protein Kinase (PKA). (2232)

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Proc. Natl. Acad. Sci. USA 94, 11055-11060. Protein phosphatase 2C dephosphorylates and inactivates cystic fibrosis transmembrane conductance regulator 1997

Travis, S.M., Berger, H.A., Welsh, M.J.

Notes: The cAMP-Dependent Protein Kinase (PKA) Catalytic Subunit was used to prepare substrates for phosphatase assays. Casein, cystic fibrosis transmembrane regulator protein (CFTR) and the R domain of the CFTR were phosphorylated by the enzyme. (0279)

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