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Protein kinase, cAMP-dependent, catalytic, beta

PRKACB, PKA Cbeta, cAMP-dependent protein kinase C beta, cAMP-dependent protein kinase catalytic beta subunit, protein kinase A catalytic subunit beta, cAMP-dependent protein kinase catalytic 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 a member of the Ser/Thr protein kinase family and is a catalytic subunit of cAMP-dependent protein kinase. Several alternatively spliced transcript variants encoding distinct isoforms have been observed. [provided by RefSeq, Jun 2011] (from NCBI)
Top mentioned proteins: protein kinase A catalytic subunit, OUT, AGE, CREB, ACID
Papers on PRKACB
Carney complex: an update.
Stratakis et al., Bethesda, United States. In Eur J Endocrinol, Oct 2015
Most recently, components of the complex have been associated with defects of other PKA subunits, such as the catalytic subunits PRKACA (adrenal hyperplasia) and PRKACB (pigmented spots, myxomas, pituitary adenomas).
miR-200c dampens cancer cell migration via regulation of protein kinase A subunits.
Schilling et al., Freiburg, Germany. In Oncotarget, Oct 2015
We identify and confirm two subunits of the central cellular kinase protein kinase A (PKA), namely PRKAR1A and PRKACB, to be directly regulated by miR-200c.
Genomic spectra of biliary tract cancer.
Shibata et al., Tokyo, Japan. In Nat Genet, Sep 2015
Gene fusions involving FGFR2 and PRKACA or PRKACB preferentially occurred in ICC and ECC, respectively, and the subtype-associated prevalence of actionable growth factor-mediated signals was noteworthy.
Pathway-based personalized analysis of breast cancer expression data.
Domany et al., Israel. In Mol Oncol, Aug 2015
RESULTS: We identified nine tumor subtypes; a new subclass (comprising about 7% of the samples) exhibits high deregulation in 38 PKA pathways, induced by overexpression of the gene PRKACB.
Sequence analysis of the catalytic subunit of PKA in somatotroph adenomas.
Korbonits et al., Oxford, United Kingdom. In Eur J Endocrinol, 2014
Recent studies have identified L206R mutations in the alpha catalytic subunit of protein kinase A (PRKACA) in cortisol-producing adrenocortical adenomas and amplification of the beta catalytic subunit of protein kinase A PRKACB in acromegaly associated with Carney complex.
Upregulation of miR-23b enhances the autologous therapeutic potential for degenerative arthritis by targeting PRKACB in synovial fluid-derived mesenchymal stem cells from patients.
Chang et al., Seoul, South Korea. In Mol Cells, 2014
The use of synovial fluid-derived mesenchymal stem cells (SFMSCs) obtained from patients with degenerative arthropathy may serve as an alternative therapeutic strategy in osteoarthritis (OA) and rheumatoid arthritis (RA).
A high throughput RNAi screen reveals determinants of HIV-1 activity in host kinases.
Lu et al., Shanghai, China. In Int J Clin Exp Pathol, 2013
Four genes, AK1, EphB2, PRKACB and CDK5R2, were found to specifically suppress the HIV-1 LTR activity following effective knockdown.
PRKACB is downregulated in non-small cell lung cancer and exogenous PRKACB inhibits proliferation and invasion of LTEP-A2 cells.
Tian et al., Shenyang, China. In Oncol Lett, 2013
Protein kinase cAMP-dependent catalytic β (PRKACB) is a member of the Ser/Thr protein kinase family and a key effector of the cAMP/PKA-induced signal transduction involved in numerous cellular process, including cell proliferation, apoptosis, gene transcription, metabolism and differentiation.
Analysis of over 10,000 Cases finds no association between previously reported candidate polymorphisms and ovarian cancer outcome.
Goode et al., New York City, United States. In Cancer Epidemiol Biomarkers Prev, 2013
METHODS: Twenty-seven SNPs in VHL, HGF, IL18, PRKACB, ABCB1, CYP2C8, ERCC2, and ERCC1 previously associated with ovarian cancer outcome were genotyped in 10,084 invasive cases from 28 studies from the Ovarian Cancer Association Consortium with over 37,000-observed person-years and 4,478 deaths.
Association between PKA gene polymorphism and NTDs in high risk Chinese population in Shanxi.
Zhang et al., Beijing, China. In Int J Clin Exp Pathol, 2012
RESULTS: Statistical analysis showed a significant correlation between the SNP sites rs12132032 in PRKACB and NTDs.
Evolutionary paths of the cAMP-dependent protein kinase (PKA) catalytic subunits.
Laerdahl et al., Oslo, Norway. In Plos One, 2012
The PKA catalytic subunits Cα and Cβ, encoded by the two genes PRKACA and PRKACB, respectively, are among the best understood and characterized human kinases.
Expression patterns of kinin-dependent genes in endometrial cancer.
Mazurek et al., Sosnowiec, Poland. In Int J Gynecol Cancer, 2012
Significant differential gene expression was recorded for GNB1, PRKAR1A, KRAS, MAP2K2, GNG5, MAPK1, ADCY9, GNG11, JUN, PRKCA, PRKACB, FOS, PLCB4, ADCY8, and GNG12.
Integrated analysis of whole genome exon array and array-comparative genomic hybridization in gastric and colorectal cancer cells.
Nishio et al., Ōsaka, Japan. In Cancer Sci, 2012
Regarding alternative splicing patterns, several cancer cell lines predominantly expressed isoform 1 of protein kinase A catalytic subunit beta (PRKACB).
Identification and expression analysis of three novel splice variants of protein kinase A catalytic β subunit gene in the mouse using combinatorial in silico and molecular biology approaches.
Tabish et al., Alīgarh, India. In Febs J, 2012
Studies identified three novel alternatively spliced transcript variants of the mouse protein kinase A catalytic beta subunit (Cbeta) gene designated Cbeta5, Cbeta6 and Cbeta7.
Association between LRRK2 and 4E-BP1 protein levels in normal and malignant cells.
Ramón y Cajal et al., Barcelona, Spain. In Oncol Rep, 2012
Several kinases affecting 4E-BP1 stability (LRRK2, RAF-1, p38γ, GSK3β, AMPKα, PRKACA and PRKACB) and 4E-BP1 phosphorylation (CDK1, PDK1, SRC, PRKCB1, PAK2, p38β, PRKCA and CaMKKB) were identified.
Identification and characterization of novel mutations in the human gene encoding the catalytic subunit Calpha of protein kinase A (PKA).
Skålhegg et al., Oslo, Norway. In Plos One, 2011
The genes PRKACA and PRKACB encode the principal catalytic (C) subunits of protein kinase A (PKA) Cα and Cβ, respectively.
Differential role of PKA catalytic subunits in mediating phenotypes caused by knockout of the Carney complex gene Prkar1a.
Kirschner et al., Columbus, United States. In Mol Endocrinol, 2011
These data suggest that both developmental and tumor phenotypes caused by Prkar1a mutation result from excess PKA activity due to PKA-Ca.
Uncoupling of bait-protein expression from the prey protein environment adds versatility for cell and tissue interaction proteomics and reveals a complex of CARP-1 and the PKA Cbeta1 subunit.
Bossemeyer et al., Heidelberg, Germany. In Proteomics, 2010
The previously unknown small molecule inhibitor-dependent interaction of Cbeta1 with the cell cycle and apoptosis regulatory protein-1 was verified.
Cross talk between phosphatidylinositol 3-kinase and cyclic AMP (cAMP)-protein kinase a signaling pathways at the level of a protein kinase B/beta-arrestin/cAMP phosphodiesterase 4 complex.
Taskén et al., Oslo, Norway. In Mol Cell Biol, 2010
Data show that PI3K activation and PIP3 production lead to recruitment of the PKB/beta-arrestin/PDE4 complex to the membrane via the PKB PH domain, resulting in degradation of the TCR-induced cAMP pool and allowing full T-cell activation to proceed.
Prostaglandin E2 induces CYP1B1 expression via ligand-independent activation of the ERalpha pathway in human breast cancer cells.
Jeong et al., Taejŏn, South Korea. In Toxicol Sci, 2010
PGE(2)-induced CYP1B1 expression is mediated by ligand-independent activation of the ERalpha pathway as a result of the activation of ERK, Akt, and PKA in breast cancer cells.
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