A type II cAMP-dependent protein kinase regulatory subunit that plays a role in confering CYCLIC AMP activation of protein kinase activity. It has a higher affinity for cAMP than that of the CYCLIC-AMP-DEPENDENT PROTEIN KINASE RIIBETA SUBUNIT. Binding of this subunit by A KINASE ANCHOR PROTEINS may play a role in the cellular localization of type II protein kinase A.
An adenine nucleotide containing one phosphate group which is esterified to both the 3'- and 5'-positions of the sugar moiety. It is a second messenger and a key intracellular regulator, functioning as a mediator of activity for a number of hormones, including epinephrine, glucagon, and ACTH.
A family of enzymes that catalyze the conversion of ATP and a protein to ADP and a phosphoprotein.
An serine-threonine protein kinase that requires the presence of physiological concentrations of CALCIUM and membrane PHOSPHOLIPIDS. The additional presence of DIACYLGLYCEROLS markedly increases its sensitivity to both calcium and phospholipids. The sensitivity of the enzyme can also be increased by PHORBOL ESTERS and it is believed that protein kinase C is the receptor protein of tumor-promoting phorbol esters.
A group of enzymes that are dependent on CYCLIC AMP and catalyze the phosphorylation of SERINE or THREONINE residues on proteins. Included under this category are two cyclic-AMP-dependent protein kinase subtypes, each of which is defined by its subunit composition.
The introduction of a phosphoryl group into a compound through the formation of an ester bond between the compound and a phosphorus moiety.
A CALMODULIN-dependent enzyme that catalyzes the phosphorylation of proteins. This enzyme is also sometimes dependent on CALCIUM. A wide range of proteins can act as acceptor, including VIMENTIN; SYNAPSINS; GLYCOGEN SYNTHASE; MYOSIN LIGHT CHAINS; and the MICROTUBULE-ASSOCIATED PROTEINS. (From Enzyme Nomenclature, 1992, p277)
A cyclic AMP-dependent protein kinase subtype primarily found in particulate subcellular fractions. They are tetrameric proteins that contain two catalytic subunits and two type II-specific regulatory subunits.
Agents that inhibit PROTEIN KINASES.
Conversion of an inactive form of an enzyme to one possessing metabolic activity. It includes 1, activation by ions (activators); 2, activation by cofactors (coenzymes); and 3, conversion of an enzyme precursor (proenzyme or zymogen) to an active enzyme.
A multifunctional calcium-calmodulin-dependent protein kinase subtype that occurs as an oligomeric protein comprised of twelve subunits. It differs from other enzyme subtypes in that it lacks a phosphorylatable activation domain that can respond to CALCIUM-CALMODULIN-DEPENDENT PROTEIN KINASE KINASE.
A type I cAMP-dependent protein kinase regulatory subunit that plays a role in confering CYCLIC AMP activation of protein kinase activity. It has a lower affinity for cAMP than the CYCLIC-AMP-DEPENDENT PROTEIN KINASE RIBETA SUBUNIT.
A monomeric calcium-calmodulin-dependent protein kinase subtype that is expressed in a broad variety of mammalian cell types. Its expression is regulated by the action of CALCIUM-CALMODULIN-DEPENDENT PROTEIN KINASE KINASE. Several isoforms of this enzyme subtype are encoded by distinct genes.
A basic element found in nearly all organized tissues. It is a member of the alkaline earth family of metals with the atomic symbol Ca, atomic number 20, and atomic weight 40. Calcium is the most abundant mineral in the body and combines with phosphorus to form calcium phosphate in the bones and teeth. It is essential for the normal functioning of nerves and muscles and plays a role in blood coagulation (as factor IV) and in many enzymatic processes.
A group of enzymes that catalyzes the phosphorylation of serine or threonine residues in proteins, with ATP or other nucleotides as phosphate donors.
A group of cyclic GMP-dependent enzymes that catalyze the phosphorylation of SERINE or THREONINE residues of proteins.
Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.
The intracellular transfer of information (biological activation/inhibition) through a signal pathway. In each signal transduction system, an activation/inhibition signal from a biologically active molecule (hormone, neurotransmitter) is mediated via the coupling of a receptor/enzyme to a second messenger system or to an ion channel. Signal transduction plays an important role in activating cellular functions, cell differentiation, and cell proliferation. Examples of signal transduction systems are the GAMMA-AMINOBUTYRIC ACID-postsynaptic receptor-calcium ion channel system, the receptor-mediated T-cell activation pathway, and the receptor-mediated activation of phospholipases. Those coupled to membrane depolarization or intracellular release of calcium include the receptor-mediated activation of cytotoxic functions in granulocytes and the synaptic potentiation of protein kinase activation. Some signal transduction pathways may be part of larger signal transduction pathways; for example, protein kinase activation is part of the platelet activation signal pathway.
The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.
A structurally-diverse family of intracellular-signaling adaptor proteins that selectively tether specific protein kinase A subtypes to distinct subcellular sites. They play a role in focusing the PROTEIN KINASE A activity toward relevant substrates. Over fifty members of this family exist, most of which bind specifically to regulatory subunits of CYCLIC AMP-DEPENDENT PROTEIN KINASE TYPE II such as CAMP PROTEIN KINASE RIIALPHA or CAMP PROTEIN KINASE RIIBETA.
The rate dynamics in chemical or physical systems.
Structurally related forms of an enzyme. Each isoenzyme has the same mechanism and classification, but differs in its chemical, physical, or immunological characteristics.
A heat-stable, low-molecular-weight activator protein found mainly in the brain and heart. The binding of calcium ions to this protein allows this protein to bind to cyclic nucleotide phosphodiesterases and to adenyl cyclase with subsequent activation. Thereby this protein modulates cyclic AMP and cyclic GMP levels.
Established cell cultures that have the potential to propagate indefinitely.
A superfamily of PROTEIN-SERINE-THREONINE KINASES that are activated by diverse stimuli via protein kinase cascades. They are the final components of the cascades, activated by phosphorylation by MITOGEN-ACTIVATED PROTEIN KINASE KINASES, which in turn are activated by mitogen-activated protein kinase kinase kinases (MAP KINASE KINASE KINASES).
A type II cAMP-dependent protein kinase regulatory subunit that plays a role in confering CYCLIC AMP activation of protein kinase activity. It has a lower affinity for cAMP than the CYCLIC-AMP-DEPENDENT PROTEIN KINASE RIIALPHA SUBUNIT. Binding of this subunit by A KINASE ANCHOR PROTEINS may play a role in the cellular localization of type II protein kinase A.
A species of ciliate protozoa. It is used in biomedical research.
An intracellular signaling system involving the MAP kinase cascades (three-membered protein kinase cascades). Various upstream activators, which act in response to extracellular stimuli, trigger the cascades by activating the first member of a cascade, MAP KINASE KINASE KINASES; (MAPKKKs). Activated MAPKKKs phosphorylate MITOGEN-ACTIVATED PROTEIN KINASE KINASES which in turn phosphorylate the MITOGEN-ACTIVATED PROTEIN KINASES; (MAPKs). The MAPKs then act on various downstream targets to affect gene expression. In mammals, there are several distinct MAP kinase pathways including the ERK (extracellular signal-regulated kinase) pathway, the SAPK/JNK (stress-activated protein kinase/c-jun kinase) pathway, and the p38 kinase pathway. There is some sharing of components among the pathways depending on which stimulus originates activation of the cascade.
The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments.
Phosphotransferases that catalyzes the conversion of 1-phosphatidylinositol to 1-phosphatidylinositol 3-phosphate. Many members of this enzyme class are involved in RECEPTOR MEDIATED SIGNAL TRANSDUCTION and regulation of vesicular transport with the cell. Phosphatidylinositol 3-Kinases have been classified both according to their substrate specificity and their mode of action within the cell.
Cells propagated in vitro in special media conducive to their growth. Cultured cells are used to study developmental, morphologic, metabolic, physiologic, and genetic processes, among others.
A mitogen-activated protein kinase subfamily that regulates a variety of cellular processes including CELL GROWTH PROCESSES; CELL DIFFERENTIATION; APOPTOSIS; and cellular responses to INFLAMMATION. The P38 MAP kinases are regulated by CYTOKINE RECEPTORS and can be activated in response to bacterial pathogens.
Compounds or agents that combine with an enzyme in such a manner as to prevent the normal substrate-enzyme combination and the catalytic reaction.
A dsRNA-activated cAMP-independent protein serine/threonine kinase that is induced by interferon. In the presence of dsRNA and ATP, the kinase autophosphorylates on several serine and threonine residues. The phosphorylated enzyme catalyzes the phosphorylation of the alpha subunit of EUKARYOTIC INITIATION FACTOR-2, leading to the inhibition of protein synthesis.
Guanosine cyclic 3',5'-(hydrogen phosphate). A guanine nucleotide containing one phosphate group which is esterified to the sugar moiety in both the 3'- and 5'-positions. It is a cellular regulatory agent and has been described as a second messenger. Its levels increase in response to a variety of hormones, including acetylcholine, insulin, and oxytocin and it has been found to activate specific protein kinases. (From Merck Index, 11th ed)
A phorbol ester found in CROTON OIL with very effective tumor promoting activity. It stimulates the synthesis of both DNA and RNA.
The parts of a macromolecule that directly participate in its specific combination with another molecule.
A cytoplasmic serine threonine kinase involved in regulating CELL DIFFERENTIATION and CELLULAR PROLIFERATION. Overexpression of this enzyme has been shown to promote PHOSPHORYLATION of BCL-2 PROTO-ONCOGENE PROTEINS and chemoresistance in human acute leukemia cells.
A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.
The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.
A proline-directed serine/threonine protein kinase which mediates signal transduction from the cell surface to the nucleus. Activation of the enzyme by phosphorylation leads to its translocation into the nucleus where it acts upon specific transcription factors. p40 MAPK and p41 MAPK are isoforms.

Conservation and function of a bovine sperm A-kinase anchor protein homologous to mouse AKAP82. (1/68)

Protein kinase A regulates sperm motility through the cAMP-dependent phosphorylation of proteins. One mechanism to direct the activity of the kinase is to localize it near its protein substrates through the use of anchoring proteins. A-Kinase anchoring proteins (AKAPs) act by binding the type II regulatory subunit of protein kinase A and tethering it to a cellular organelle or cytoskeletal element. We showed previously that mAKAP82, the major protein of the fibrous sheath of the mouse sperm flagellum, is an AKAP. The available evidence indicates that protein kinase A is compartmentalized to the fibrous sheath by binding mAKAP82. To characterize AKAP82 in bovine sperm, a testicular cDNA library was constructed and used to isolate a clone encoding bAKAP82, the bovine homologue. Sequence analysis showed that the primary structure of bAKAP82 was highly conserved. In particular, the amino acid sequence corresponding to the region of mAKAP82 responsible for binding the regulatory subunit of protein kinase A was identical in the bull. Bovine AKAP82 was present in both epididymal and ejaculated sperm and was localized to the entire principal piece of the flagellum, the region in which the fibrous sheath is located. Finally, bAKAP82 bound the regulatory subunit of protein kinase A. These data support the idea that bAKAP82 functions as an anchoring protein for the subcellular localization of protein kinase A in the flagellum.  (+info)

Generation of a novel A kinase anchor protein and a myristoylated alanine-rich C kinase substrate-like analog from a single gene. (2/68)

A unique Drosophila gene encodes two novel signaling proteins. Drosophila A kinase anchor protein 200 (DAKAP200) (753 amino acids) binds regulatory subunits of protein kinase AII (PKAII) isoforms in vitro and in intact cells. The acidic DAKAP200 polypeptide (pI approximately 3.8) contains an optimal N-terminal myristoylation site and a positively charged domain that resembles the multifunctional phosphorylation site domain of vertebrate myristoylated alanine-rich C kinase substrate proteins. The 15-kilobase pair DAKAP200 gene contains six exons and encodes a second protein, DeltaDAKAP200. DeltaDAKAP200 is derived from DAKAP200 transcripts by excision of exon 5 (381 codons), which encodes the PKAII binding region and a Pro-rich sequence. DeltaDAKAP200 appears to be a myristoylated alanine-rich C kinase substrate analog. DAKAP200 and DeltaDAKAP200 are evident in vivo at all stages of Drosophila development. Thus, both proteins may play important physiological roles throughout the life span of the organism. Nevertheless, DAKAP200 gene expression is regulated. Maximal levels of DAKAP200 are detected in the pupal phase of development; DeltaDAKAP200 content is elevated 7-fold in adult head (brain) relative to other body parts. Enhancement or suppression of exon 5 excision during DAKAP200 pre-mRNA processing provides potential mechanisms for regulating anchoring of PKAII and targeting of cAMP signals to effector sites in cytoskeleton and/or organelles.  (+info)

A novel mechanism of PKA anchoring revealed by solution structures of anchoring complexes. (3/68)

The specificity of intracellular signaling events is controlled, in part, by compartmentalization of protein kinases and phosphatases. The subcellular localization of these enzymes is often maintained by protein- protein interactions. A prototypic example is the compartmentalization of the cAMP-dependent protein kinase (PKA) through its association with A-kinase anchoring proteins (AKAPs). A docking and dimerization domain (D/D) located within the first 45 residues of each regulatory (R) subunit protomer forms a high affinity binding site for its anchoring partner. We now report the structures of two D/D-AKAP peptide complexes obtained by solution NMR methods, one with Ht31(493-515) and the other with AKAP79(392-413). We present the first direct structural data demonstrating the helical nature of the peptides. The structures reveal conserved hydrophobic interaction surfaces on the helical AKAP peptides and the PKA R subunit, which are responsible for mediating the high affinity association in the complexes. In a departure from the dimer-dimer interactions seen in other X-type four-helix bundle dimeric proteins, our structures reveal a novel hydrophobic groove that accommodates one AKAP per RIIalpha D/D.  (+info)

Binding of PKA-RIIalpha to the Adenovirus E1A12S oncoprotein correlates with its nuclear translocation and an increase in PKA-dependent promoter activity. (4/68)

The adenovirus type 12 (Ad12) E1A12S oncoprotein utilizes the cAMP/protein kinase A (PKA) signal transduction pathway to activate expression of the viral E2 gene, the products of which are essential for viral replication. A central unsolved question is, however, whether E1A12S interacts directly with PKA in the process of promoter activation. We show here that E1A12S binds to the regulatory subunits (R) of PKA in vitro and in vivo. Interaction depends on the N-terminus and the conserved region 1 (CR1) of E1A12S. Both domains are also essential for the activation of viral E2 gene expression. Infection of cells with Ad12 leads to the cellular redistribution of RIIalpha from the cytoplasm into the nucleus. Furthermore, RIIalpha is also located in the nucleus of cells transformed by E1 of Ad12 and transient expression of E1A12S leads to the redistribution of RIIalpha into the nucleus in a N-terminus- and CR1-dependent manner. Cotransfection of E1A12S with RIIalpha results in strong activation of the E2 promoter. Based on these results we conclude that E1A12S functions as a viral A-kinase anchoring protein redistributing RIIalpha from the cytoplasm into the nucleus where it is involved in E1A12S-mediated activation of the E2 promoter.  (+info)

CDK1-mediated phosphorylation of the RIIalpha regulatory subunit of PKA works as a molecular switch that promotes dissociation of RIIalpha from centrosomes at mitosis. (5/68)

Protein kinase A regulatory subunit RIIalpha is tightly bound to centrosomal structures during interphase through interaction with the A-kinase anchoring protein AKAP450, but dissociates and redistributes from centrosomes at mitosis. The cyclin B-p34(cdc2) kinase (CDK1) has been shown to phosphorylate RIIalpha on T54 and this has been proposed to alter the subcellular localization of RIIalpha. We have made stable transfectants from an RIIalpha-deficient leukemia cell line (Reh) that expresses either wild-type or mutant RIIalpha (RIIalpha(T54E)). When expressed, RIIalpha detaches from centrosomes at mitosis and dissociates from its centrosomal location in purified nucleus-centrosome complexes by incubation with CDK1 in vitro. By contrast, centrosomal RIIalpha(T54E) is not redistributed at mitosis, remains mostly associated with centrosomes during all phases of the cell cycle and cannot be solubilized by CDK1 in vitro. Furthermore, RIIalpha is solubilized from particular cell fractions and changes affinity for AKAP450 in the presence of CDK1. D and V mutations of T54 also reduce affinity for the N-terminal RII-binding domain of AKAP450, whereas small neutral residues do not change affinity detected by surface plasmon resonance. In addition, only RIIalpha(T54E) interacts with AKAP450 in a RIPA-soluble extract from mitotic cells. Finally, microtubule repolymerization from mitotic centrosomes of the RIIalpha(T54E) transfectant is poorer and occurs at a lower frequency than that of RIIalpha transfectants. Our results suggest that T54 phosphorylation of RIIalpha by CDK1 might serve to regulate the centrosomal association of PKA during the cell cycle.  (+info)

Regulation of anchoring of the RIIalpha regulatory subunit of PKA to AKAP95 by threonine phosphorylation of RIIalpha: implications for chromosome dynamics at mitosis. (6/68)

CDK1 phosphorylates the A-kinase regulatory subunit RIIalpha on threonine 54 (T54) at mitosis, an event proposed to alter the subcellular localization of RIIalpha. Using an RIIalpha-deficient leukemic cell line (Reh) and stably transfected Reh cell clones expressing wild-type RIIalpha or an RIIalpha(T54E) mutant, we show that RIIalpha associates with chromatin-bound A-kinase anchoring protein AKAP95 at mitosis and that this interaction involves phosphorylation of RIIalpha on T54. During interphase, both RIIalpha and RIIalpha(T54E) exhibit a centrosome-Golgi localization, whereas AKAP95 is intranuclear. At mitosis and in a mitotic extract, most RIIalpha, but not RIIalpha(T54E), co-fractionates with chromatin, onto which it associates with AKAP95. This correlates with T54 phosphorylation of RIIalpha. Disrupting AKAP95-RIIalpha anchoring or depleting RIIalpha from the mitotic extract promotes premature chromatin decondensation. In a nuclear reconstitution assay that mimics mitotic nuclear reformation, RIIalpha is threonine dephosphorylated and dissociates from AKAP95 prior to assembly of nuclear membranes. Lastly, the Reh cell line exhibits premature chromatin decondensation in vitro, which can be rescued by addition of wild-type RIIalpha or an RIIalpha(T54D) mutant, but not RIIalpha(T54E, A, L or V) mutants. Our results suggest that CDK1-mediated T54 phosphorylation of RIIalpha constitutes a molecular switch controlling anchoring of RIIalpha to chromatin-bound AKAP95, where the PKA-AKAP95 complex participates in remodeling chromatin during mitosis.  (+info)

Positive regulation of cell-cell and cell-substrate adhesion by protein kinase A. (7/68)

Integrin receptor activation is an important regulatory mechanism for cell-substrate and cell-cell adhesion. In this study, we explore a signaling pathway activated by mAb 12G10, an antibody that can activate beta(1) integrins and induce integrin-mediated cell-cell and cell-substrate adhesion. We have found that the cAMP-dependent protein kinase (PKA) is required for both mAb 12G10-induced cell-cell and cell-substrate adhesion of HT-1080 cells. Binding of mAb 12G10 to beta(1) integrins stimulates an increase in intracellular cAMP levels and PKA activity, and a concomitant shift in the localization of the PKA type II regulatory subunits from the cytoplasm to areas where integrins expressing the 12G10 epitope are located. MAb 12G10-induced cell-cell adhesion was mimicked by a combination of clustering beta(1) integrins and elevating PKA activity with Sp-adenosine-3',5'-cyclic monophosphorothioate or forskolin. We also show that two processes required for HT-1080 cell-cell adhesion, integrin clustering and F-actin polymerization are both dependent on PKA. Taken together, our data suggest that PKA plays a key role in the signaling pathway, resulting from activation of beta(1) integrins, and that this enzyme may be required for upregulation of cell-substrate and cell-cell adhesion.  (+info)

Evidence for involvement of A-kinase anchoring protein in activation of rat arterial K(ATP) channels by protein kinase A. (8/68)

1. We have investigated the possible role of A-kinase anchoring proteins (AKAPs) in protein kinase A (PKA) signalling to ATP-sensitive K+ (K(ATP)) channels of rat isolated mesenteric arterial smooth muscle cells using whole-cell patch clamp and peptides that inhibit PKA-AKAP binding. 2. Intracellular Ht31 peptide (20 microM), which inhibits the PKA-AKAP interaction, blocked K(ATP) current activation by either dibutyryl cAMP or calcitonin gene-related peptide. Ht31-proline (20 microM), which does not inhibit PKA binding to AKAP, did not block K(ATP) current activation. 3. Ht31 reduced K(ATP) current activated by pinacidil and also prevented its inhibition by Rp-cAMPS, effects consistent with Ht31 blocking steady-state K(ATP) channel activation by PKA. However, Ht31 did not prevent K(ATP) current activation by the catalytic subunit of PKA. 4. An antibody to the RII subunit of PKA showed localization of PKA near to the cell membrane. Our results provide evidence that both steady-state and receptor-driven activation of K(ATP) channels by PKA involve the localization of PKA by an AKAP.  (+info)

... type-II regulatory subunit of cyclic-AMP-dependent protein kinase by glycogen synthase kinase 3 and glycogen synthase kinase 5 ... and characterization of subunits of cAMP-dependent protein kinase in human testis. Reverse mobilities of human RII alpha and ... "MTG8 proto-oncoprotein interacts with the regulatory subunit of type II cyclic AMP-dependent protein kinase in lymphocytes". ... "Ezrin is a cyclic AMP-dependent protein kinase anchoring protein". The EMBO Journal. 16 (1): 35-43. doi:10.1093/emboj/16.1.35. ...
Cyclic-AMP-Dependent Protein Kinase RIIalpha Subunit Protein Kinase A, RII alpha Subunit RII alpha, cAMP Protein Kinase ... RIIalpha, cAMP Protein Kinase Regulatory Subunit RIIalpha, Cyclic-AMP-Dependent Protein Kinase cAMP Protein Kinase RIIalpha ... Cyclic AMP-Dependent Protein Kinase RIIalpha Subunit [D12.776.476.563.150.125.875.750] * Cyclic AMP-Dependent Protein Kinase ... 2008; CAMP-DEPENDENT PROTEIN KINASE, TYPE 2ALPHA-REGULATORY SUBUNIT (now CYCLIC-AMP-DEPENDENT PROTEIN KINASE RIIALPHA SUBUNIT) ...
Cyclic AMP Dependent Protein Kinase RIIalpha Subunit Cyclic-AMP-Dependent Protein Kinase RIIalpha Subunit Protein Kinase A, RII ... Cyclic AMP Dependent Protein Kinase RIIalpha Subunit. Cyclic-AMP-Dependent Protein Kinase RIIalpha Subunit. Protein Kinase A, ... Cyclic AMP Dependent Protein Kinase Regulatory Subunit RIIalpha, Cyclic-AMP-Dependent Protein Kinase cAMP Dependent Protein ... Cyclic AMP Dependent Protein Kinase. Regulatory Subunit RIIalpha, Cyclic-AMP-Dependent Protein Kinase. cAMP Dependent Protein ...
Cyclic-AMP-Dependent Protein Kinase RIIalpha Subunit Protein Kinase A, RII alpha Subunit RII alpha, cAMP Protein Kinase ... RIIalpha, cAMP Protein Kinase Regulatory Subunit RIIalpha, Cyclic-AMP-Dependent Protein Kinase cAMP Protein Kinase RIIalpha ... Cyclic AMP-Dependent Protein Kinase RIIalpha Subunit [D12.776.476.563.150.125.875.750] * Cyclic AMP-Dependent Protein Kinase ... 2008; CAMP-DEPENDENT PROTEIN KINASE, TYPE 2ALPHA-REGULATORY SUBUNIT (now CYCLIC-AMP-DEPENDENT PROTEIN KINASE RIIALPHA SUBUNIT) ...
... subunits of CYCLIC-AMP-DEPENDENT PROTEIN KINASE TYPE II such as CAMP PROTEIN KINASE RIIALPHA or CAMP PROTEIN KINASE RIIBETA. HN ... Protein Kinase A, Type I BX - Protein Kinase Type I, Cyclic AMP-Dependent MH - Cyclic AMP-Dependent Protein Kinase Type II UI ... HN - 2008(1998) BX - Protein Kinase A, RIbeta Subunit MH - Cyclic AMP-Dependent Protein Kinase RIIalpha Subunit UI - D054754 MN ... Protein Kinase A, RII alpha Subunit MH - Cyclic AMP-Dependent Protein Kinase RIIbeta Subunit UI - D054757 MN - D8.811.913.696. ...
Dependent Protein Kinase RIbeta Subunit N0000178692 Cyclic AMP-Dependent Protein Kinase RIIalpha Subunit N0000178693 Cyclic AMP ... Protein Kinase RIIbeta Subunit N0000178794 Cyclic AMP-Dependent Protein Kinase Type I N0000178580 Cyclic AMP-Dependent Protein ... Protein A N0000178795 Cyclic AMP-Dependent Protein Kinase Catalytic Subunits N0000178690 Cyclic AMP-Dependent Protein Kinase ... Protein Kinase Type I N0000185712 Cyclic GMP-Dependent Protein Kinase Type II N0000170597 Cyclic GMP-Dependent Protein Kinases ...
Protein Kinase Type II, Cyclic AMP-Dependent MH - Cyclic AMP-Dependent Protein Kinase RIIalpha Subunit UI - D054754 MN - ... Protein Kinase A, Type I BX - Protein Kinase Type I, Cyclic AMP-Dependent MH - Cyclic AMP-Dependent Protein Kinase Catalytic ... protein kinase A. HN - 2008(1998) BX - Protein Kinase A, RII alpha Subunit MH - Cyclic AMP-Dependent Protein Kinase RIIbeta ... CYCLIC-AMP-DEPENDENT PROTEIN KINASE TYPE II such as CAMP PROTEIN KINASE RIIALPHA or CAMP PROTEIN KINASE RIIBETA. HN - 2008 MH ...
The main function of the A kinase-anchoring proteins (AKAPs) is to target the cyclic AMP-dependent protein kinase A (PKA) to ... We further demonstrate that AKAP8 interacts with DPY30 and the RII alpha regulatory subunit of PKA both in the interphase and ... dependent protein kinase Iα (PKG Iα) and adenosine 3,5-cyclic monophosphate (cAMP)-dependent protein kinase (PKA) isoenzymes ... The Activation of Protein Kinase A by the Calcium-Binding Protein S100A1 Is Independent of Cyclic AMP. ...
Cyclic AMP-Dependent Protein Kinase RIIalpha Subunit. Subunidad de Proteína Quinasa RIIalfa Dependiente de AMP Cíclico. ... Cyclic AMP-Dependent Protein Kinase RIIbeta Subunit. Subunidad de Proteína Quinasa RIIbeta Dependiente de AMP Cíclico. ... Cyclic AMP-Dependent Protein Kinase RIalpha Subunit. Subunidad de Proteína Quinasa RIalfa Dependiente de AMP Cíclico. ... Cyclic AMP-Dependent Protein Kinase RIbeta Subunit. Subunidad de Proteína Quinasa RIbeta Dependiente de AMP Cíclico. ...
Cyclic AMP-Dependent Protein Kinase RIbeta Subunit Cyclic AMP-Dependent Protein Kinase RIIalpha Subunit Cyclic AMP-Dependent ... Cyclic AMP-Dependent Protein Kinase Type I Cyclic AMP-Dependent Protein Kinase Type II Cyclic AMP-Dependent Protein Kinases ... Cyclic AMP Response Element-Binding Protein A Cyclic AMP-Dependent Protein Kinase Catalytic Subunits Cyclic AMP-Dependent ... Cyclic GMP Cyclic GMP-Dependent Protein Kinase Type I Cyclic GMP-Dependent Protein Kinase Type II Cyclic GMP-Dependent Protein ...
Cyclic AMP-Dependent Protein Kinase RIIalpha Subunit / genetics Actions. * Search in PubMed ... coding for the inhibitory regulatory subunit of PKA) at 3p21, leading to a high PRKACA/PRKAR2A ratio at the mRNA and protein ... Cyclic AMP-Dependent Protein Kinase Catalytic Subunits / genetics* Actions. * Search in PubMed ... DNAJB1-PRKACA fusion kinase interacts with β-catenin and the liver regenerative response to drive fibrolamellar hepatocellular ...
Cyclic AMP-Dependent Protein Kinase RIIalpha Subunit. Subunidade RIIalfa da Proteína Quinase Dependente de AMP Cíclico. ... Cyclic AMP-Dependent Protein Kinase RIbeta Subunit. Subunidade RIbeta da Proteína Quinase Dependente de AMP Cíclico. Subunidad ... Cyclic AMP-Dependent Protein Kinase RIalpha Subunit. Subunidade RIalfa da Proteína Quinase Dependente de AMP Cíclico. Subunidad ... Cyclic AMP-Dependent Protein Kinase Catalytic Subunits. Subunidades Catalíticas da Proteína Quinase Dependente de AMP Cíclico. ...
... protein time point with acid nos oral other quantitative concentration for gene product left antibody right tablet serum ... fire foley metal leukocytes challenge deformity ile bromo valyl plant ureter coated tests diabetes action cyclic encourage ... resectable crps dipi lawsonia gra5 cycloidea ffp enriching neoadjuvant pok gal6 rab17 reggie luteolytic rhp54 riialpha xpsd ... length normal pulmonary breast therapy abdominal vertebral name peptide collision membrane limb enzyme partial potassium kinase ...
  • A type II cAMP-dependent protein kinase regulatory subunit that plays a role in confering CYCLIC AMP activation of protein kinase activity. (nih.gov)
  • Over fifty members of this family exist, most of which bind specifically to regulatory subunits of CYCLIC-AMP-DEPENDENT PROTEIN KINASE TYPE II such as CAMP PROTEIN KINASE RIIALPHA or CAMP PROTEIN KINASE RIIBETA. (nih.gov)
  • Protein kinase A, particularly its regulatory subunit R2Alpha, presents a typical intracellular distribution in glioblastoma cells compared to the healthy brain parenchyma and this peculiarity might be exploited in a therapeutic setting. (bvsalud.org)
  • In the present study, a third-generation lentiviral system for delivery of shRNA targeting the regulatory subunit R2Alpha of protein kinase A was developed. (bvsalud.org)
  • In addition, our data suggest a potential correlation between silencing of the regulatory subunit of protein kinase A and reduced viability of tumor cells, apparently due to a reduction in replication rate. (bvsalud.org)
  • HN - 2008 BX - Child Abuse, Adult Survivors MH - Agouti Signaling Protein UI - D054366 MN - D12.644.276.49 MN - D12.776.467.49 MN - D23.529.49 MS - A secreted protein of approximately 131 amino acids (depending on species) that regulates the synthesis of eumelanin (brown/black) pigments in MELANOCYTES. (nih.gov)
  • HN - 2008 (1993) MH - Agouti-Related Protein UI - D054369 MN - D12.644.276.74 MN - D12.776.467.74 MN - D23.529.74 MS - A secreted protein of approximately 131 amino acids that is related to AGOUTI SIGNALING PROTEIN and is also an antagonist of MELANOCORTIN RECEPTOR activity. (nih.gov)
  • Binding of this subunit by A KINASE ANCHOR PROTEINS may play a role in the cellular localization of type II protein kinase A. (nih.gov)
  • They play a role in focusing the PROTEIN KINASE A activity toward relevant substrates. (nih.gov)
  • Here, we asked whether glucose affects posttranscriptional steps and regulates protein synthesis in human ß-cell lines. (bvsalud.org)
  • Thus, our findings support the role of protein kinase A as a promising target for novel anti-glioma therapies. (bvsalud.org)