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)

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)

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)

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)

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)

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)

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

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)

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

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)

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)

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

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)

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)

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)

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

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)