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Data (including data from studies using knockout mice) suggest that S100A1 (zeige S100A1 Proteine) (S-100 calcium-binding protein (zeige GUCA1B Proteine) A1 (zeige BCL2A1 Proteine), alpha chain (zeige FCGRT Proteine)) is involved in protein kinase A- (RIIalpha and RIIbeta)-dependent signaling resulting in nuclear redistribution/influx of HDAC4 (histone deacetylase 4 (zeige HDAC5 Proteine)) in skeletal muscle fibers.
RIIbeta-PKA modulates the duration of leptin receptor (zeige LEPR Proteine) signalling and therefore the magnitude of the catabolic response to leptin (zeige LEP Proteine).
RIIBeta protein kinase A knockout was protective against induced seizure susceptibility.
Deficiency of the RIIbeta subunit of PKA affects locomotor activity and energy homeostasis in distinct neuronal populations.
study describes the 2.3 angstrom structure of full-length tetrameric RIIbeta(2):C(2) holoenzyme
Conditioned taste aversion (CTA (zeige PCYT1A Proteine)) learning was examined in mice with a targeted disruption of a gene for a specific regulatory subunit of PKA (RIIbeta), which is selectively expressed in amygdala. Disruption of PKA signaling interferes with CTA (zeige PCYT1A Proteine).
RII-PKAII complements TSHR (zeige TSHR Proteine) action by stably propagating robust cAMP signals in cell compartments
Here we show that visual cortical plasticity remains intact in AC1 (zeige HRASLS Proteine)/AC8 (zeige ADCY8 Proteine)-/- mice, whereas Ocular dominance plasticity and LTD, but not LTP (zeige SCP2 Proteine), are absent in RIIbeta-/- mice
Disruption of the RIIbeta regulatory subunit of protein kinase A (PKA) results in mice with a lean phenotype, nocturnal hyperactivity, and increased resting metabolic rate.
increased ingestion of ethanol by protein kinase A(PKA) subunit RIIbeta(-/-) mice is likely the result of altered PKA activity within neuronal pathways that control ethanol-consummatory behaviors
Leu206Arg and Leu199_Cys200insTrp mutations in PRKACA (zeige PRKACA Proteine) impair its association with PRKAR2B and PRKAR1A (zeige PRKAR1A Proteine).
Although the depletion of PRKAR1A (zeige PRKAR1A Proteine) and PRKAR2B in adrenocortical cells has similar effects on cell proliferation and apoptosis; loss of these PKA subunits differentially affects cyclin (zeige PCNA Proteine) expression.
Because of limited power, PRKAR2B's role in antipsychotic-induced weight gain is unclear, but biological evidence suggests that PRKAR2B may be involved
lipolytic catecholamine resistance of sc adipocytes in polycystic ovary syndrome is probably due to a combination of decreased amounts of beta(2)-adrenergic receptors, the regulatory II beta-component of protein kinase A, and hormone-sensitive lipase (zeige LIPE Proteine)
Nuclear RII beta can act as a repressor of CREB (zeige CREB1 Proteine) transcriptional activity in T cells, providing a potential functional significance for aberrant levels of nuclear RII beta in systemic lupus erythematosus T cells.
there are abnormalities in [3H]cAMP binding and catalytic activity kinase A in brain of depressed suicide victims, which could be due to reduced expression of RIIbeta and Cbeta
serine 114 phosphorylation and nuclear localization of RIIbeta controls the regulation of IL-2 (zeige IL2 Proteine) gene expression in T cells.
Loss of PRKAR2B protein due to a post-transcriptional mechanism in ACA-S is a new mechanism of cAMP pathway dysregulation in adrenocortical tumorigenesis.
PKA RII(beta) is responsible for increased glucocorticoid sensitivity, critical for cAMP-mediated synergistic cell killing in CEM cells
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
angle X-ray scattering studies indicate that the RIalpha (zeige PRKAR1A Proteine), RIIalpha, and RIIbeta homodimers differ markedly in overall shape, despite extensive sequence homology and similar molecular masses
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.
protein kinase, cAMP-dependent, regulatory, type II, beta
, cAMP-dependent protein kinase, regulatory subunit beta 2
, cAMP-dependent protein kinase type II-beta regulatory subunit-like
, protein kinase, cAMP dependent regulatory, type II beta
, cAMP-dependent protein kinase type II-beta regulatory subunit
, Type II beta regulatory subunit of cAMP-dependent protein kinase
, cAMP-dependent protein kinase type II-beta regulatory chain