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Protein kinase, cAMP-dependent, catalytic, gamma

PRKACG, serine(threonine) protein kinase, cAMP-dependent protein kinase catalytic subunit C alpha
Cyclic AMP-dependent protein kinase (PKA) consists of two catalytic subunits and a regulatory subunit dimer. This gene encodes the gamma form of its catalytic subunit. The gene is intronless and is thought to be a retrotransposon derived from the gene for the alpha form of the PKA catalytic subunit. [provided by RefSeq, Jul 2008] (from NCBI)
Papers on PRKACG
Overexpressing PKIB in prostate cancer promotes its aggressiveness by linking between PKA and Akt pathways.
Nakagawa et al., Tokyo, Japan. In Oncogene, 2009
Findings show that PKIB and PKA-C kinase can have critical functions of aggressive phenotype of PCs through Akt phosphorylation and that they should be a promising molecular target for PC treatment.
PKA-mediated stabilization of FoxH1 negatively regulates ERalpha activity.
Yeo et al., Seoul, South Korea. In Mol Cells, 2009
Results suggest that PKA can negatively regulate ERalpha, at least in part, through FoxH1.
The paradoxical increase in cortisol secretion induced by dexamethasone in primary pigmented nodular adrenocortical disease involves a glucocorticoid receptor-mediated effect of dexamethasone on protein kinase A catalytic subunits.
Lefebvre et al., Mont-Saint-Aignan, France. In J Clin Endocrinol Metab, 2009
In human primary pigmented nodular adrenocortical disease tissues, dexamethasone paradoxically stimulates cortisol release through a glucocorticoid receptor-mediated effect on PKA catalytic subunits.
Mutation in the catalytic domain of protein kinase C gamma and extension of the phenotype associated with spinocerebellar ataxia type 14.
Durr et al., Paris, France. In Arch Neurol, 2004
A novel missense mutation, F643L, which maps to a highly conserved amino acid of the catalytic domain of protein kinase C gamma, extends the phenotype associated with the spinocerebellar ataxia type 14 (SCA14) locus.
Characterization of the cAMP-dependent protein kinase catalytic subunit Cgamma expressed and purified from sf9 cells.
Beebe et al., Chicago, United States. In Protein Expr Purif, 2004
Results suggest that Cgamma and Calpha differ in structure and function in vitro, supporting the hypothesis that functionally different C-subunit isozymes could affect cAMP signal transduction downstream of protein kinase A activation.
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