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Protein kinase, cAMP-dependent, regulatory, type II, beta

cAMP is a signaling molecule important for a variety of cellular functions. cAMP exerts its effects by activating the cAMP-dependent protein kinase, which transduces the signal through phosphorylation of different target proteins. The inactive kinase holoenzyme is a tetramer composed of two regulatory and two catalytic subunits. cAMP causes the dissociation of the inactive holoenzyme into a dimer of regulatory subunits bound to four cAMP and two free monomeric catalytic subunits. Four different regulatory subunits and three catalytic subunits have been identified in humans. The protein encoded by this gene is one of the regulatory subunits. This subunit can be phosphorylated by the activated catalytic subunit. This subunit has been shown to interact with and suppress the transcriptional activity of the cAMP responsive element binding protein 1 (CREB1) in activated T cells. Knockout studies in mice suggest that this subunit may play an important role in regulating energy balance and adiposity. The studies also suggest that this subunit may mediate the gene induction and cataleptic behavior induced by haloperidol. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: CAN, HAD, ACID, V1a, CREB
Papers on RIIbeta
Haploinsufficiency for either one of the type-II regulatory subunits of protein kinase A improves the bone phenotype of Prkar1a+/- mice.
Stratakis et al., Bethesda, United States. In Hum Mol Genet, Dec 2015
Tumor tissues in these animals had increased PKA activity due to an unregulated PKA catalytic subunit and increased PKA type II (PKA-II) activity mediated by the PRKAR2A and PRKAR2B subunits.
miR-200c dampens cancer cell migration via regulation of protein kinase A subunits.
Schilling et al., Freiburg, Germany. In Oncotarget, Oct 2015
By bioinformatics, we define a miRNA target cluster consisting of PRKAR1A, PRKAR2B, PRKACB, and COF2, which is targeted by a group of 14 miRNAs.
Different expression of protein kinase A (PKA) regulatory subunits in normal and neoplastic thyroid tissues.
Lania et al., Milano, Italy. In Histol Histopathol, Apr 2015
Immunohistochemistry demonstrated a significant increase in PRKAR2B expression in both differentiated and undifferentiated (anaplastic) thyroid tumors in comparison with normal thyroid tissues.
Evaluation of drug-targetable genes by defining modes of abnormality in gene expression.
Choi et al., Taejŏn, South Korea. In Sci Rep, 2014
Computationally, PTPRF, PRKAR2B, MAP4K3, and RICTOR were calculated as highly drug-targetable genes for breast cancer.
Hematopoietic neoplasms in Prkar2a-deficient mice.
Stratakis et al., Bethesda, United States. In J Exp Clin Cancer Res, 2014
Mice with inactivation of the Prkar2a and Prkar2b genes (coding for RIIα and RIIβ, respectively) are also viable but have not been studied for their susceptibility to any tumors.
Comparison of the effects of PRKAR1A and PRKAR2B depletion on signaling pathways, cell growth, and cell cycle control of adrenocortical cells.
Rizk-Rabin et al., Paris, France. In Horm Metab Res, 2014
We previously showed that PRKAR1A and PRKAR2B inactivation have anti-apoptotic effects on the adrenocortical carcinoma cell line H295R.
Protein kinase cAMP-dependent regulatory type II beta (PRKAR2B) gene variants in antipsychotic-induced weight gain.
Müller et al., Toronto, Canada. In Hum Psychopharmacol, 2014
Mouse and human studies suggest that the protein kinase cAMP-dependent regulatory type II beta (PRKAR2B) gene may be involved in energy metabolism, and there is evidence that it is associated with clozapine's effects on triglyceride levels.
Expression and molecular consequences of inhibition of estrogen receptors in granulosa cells of bovine follicles.
Gonçalves et al., Santa Maria, Brazil. In J Ovarian Res, 2013
Analyses of FSH-regulated genes revealed that ESRs inhibition in the dominant follicle decreased the transcript levels of the GJA1 but not those of PRKAR2B, MRO or LRP11 genes.
PKA regulatory subunit R2B is required for murine and human adipocyte differentiation.
Mantovani et al., Erba, Italy. In Endocr Connect, 2012
Protein kinase A alterations in endocrine tumors.
Bertherat et al., Paris, France. In Horm Metab Res, 2012
So far, most alterations have been observed for the regulatory subunits, mainly PRKAR1A and to a lower extent, PRKAR2B.
cAMP-dependent protein kinase A (PKA) signaling induces TNFR1 exosome-like vesicle release via anchoring of PKA regulatory subunit RIIbeta to BIG2.
Levine et al., Bethesda, United States. In J Biol Chem, 2008
both the constitutive and cAMP-induced release of TNFR1 exosome-like vesicles occur via PKA-dependent pathways that are regulated by the anchoring of RIIbeta to BIG2 via AKAP domains B and C
Detection of protein biomarkers using high-throughput immunoblotting following focal ischemic or penetrating ballistic-like brain injuries in rats.
Dave et al., Silver Spring, United States. In Brain Inj, 2008
Western blots were used to verify HTPI results for selected proteins with measurable changes observed in both blood and brain for the proteins STAT3, Tau, PKA RII beta, 14-3-3 epsilon and p43/EMAPII.
Protein kinase A (PKA) isoform RIIbeta mediates the synergistic killing effect of cAMP and glucocorticoid in acute lymphoblastic leukemia cells.
Cheng et al., Galveston, United States. In J Biol Chem, 2008
PKA RII(beta) is responsible for increased glucocorticoid sensitivity, critical for cAMP-mediated synergistic cell killing in CEM cells
Identification of a clinically homogenous subgroup of benign cortisol-secreting adrenocortical tumors characterized by alterations of the protein kinase A (PKA) subunits and high PKA activity.
Bertherat et al., Paris, France. In Eur J Endocrinol, 2008
Loss of PRKAR2B protein due to a post-transcriptional mechanism in ACA-S is a new mechanism of cAMP pathway dysregulation in adrenocortical tumorigenesis.
Different expression of protein kinase A (PKA) regulatory subunits in cortisol-secreting adrenocortical tumors: relationship with cell proliferation.
Spada et al., Milano, Italy. In Exp Cell Res, 2008
A high R1/R2 ratio favors the proliferation of well differentiated and hormone producing adrenocortical cells, while unbalanced expression of these subunits is not required for malignant transformation.
Psychosis pathways converge via D2high dopamine receptors.
Sumiyoshi et al., Toronto, Canada. In Synapse, 2006
Mice born with gene knockouts of some possible schizophrenia susceptibility genes are dopamine supersensitive, and their striata reveal markedly elevated D2High states; suchgenes include dopamine-beta-hydroxylase, dopamine D4 receptors, G protein receptor kinase 6, tyrosine hydroxylase, catechol-O-methyltransferase, the trace amine-1 receptor, regulator of G protein signaling RGS9, and the RIIbeta form of cAMP-dependent protein kinase (PKA).
Chemoprevention with protein kinase A RIalpha antisense in DMBA-mammary carcinogenesis.
Cho-Chung et al., Bethesda, United States. In Ann N Y Acad Sci, 2005
The effect of RIalpha antisense oligonucleotide correlated with a decrease in RIalpha protein and a concomitant increase in RIIbeta protein level.
Tumor reversion: protein kinase A isozyme switching.
Nesterova et al., Bethesda, United States. In Ann N Y Acad Sci, 2005
DNA microarrays demonstrate that antisense suppression of the RIalpha, which upregulates RIIbeta, downregulates a wide range of genes involved in cell proliferation and transformation while upregulating cell differentiation and reverse transformation genes in PC3M prostate tumors that undergo regression.
Down-regulation of IL-2 production in T lymphocytes by phosphorylated protein kinase A-RIIbeta.
Kammer et al., Winston-Salem, United States. In J Immunol, 2004
serine 114 phosphorylation and nuclear localization of RIIbeta controls the regulation of IL-2 gene expression in T cells.
Genetically lean mice result from targeted disruption of the RII beta subunit of protein kinase A.
McKnight et al., Seattle, United States. In Nature, 1996
In mice there are four R genes (encoding RI alpha, RI beta, RII alpha, and RII beta) and two C gene (encoding C alpha and C beta), expressed in tissue-specific patterns.
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