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Human PRKACA Protein expressed in Wheat germ - ABIN1316219
Loilome, Yooyuen, Namwat, Sithithaworn, Puapairoj, Kano, Noguchi, Miwa, Yongvanit: PRKAR1A overexpression is associated with increased ECPKA autoantibody in liver fluke-associated cholangiocarcinoma: application for assessment of the risk group. in Tumour biology 2012
Ezrin (show EZR Proteins)-anchored PKA phosphorylates serine 369 and 373 on connexin 43 (show GJA1 Proteins) to enhance gap junction assembly, communication, and cell fusion.
CaV1.4 (show CACNA1F Proteins) channels are indeed modulated by PKA phosphorylation within the inhibitor of Ca(2 (show CA2 Proteins)+)-dependent inactivation (ICDI) motif.
In this study, the authors linked for the first time the loss of RIIbeta (show PRKAR2B Proteins) protein levels to the PRKACA mutation status and found the down-regulation of RIIbeta (show PRKAR2B Proteins) to arise post-transcriptionally.
the presence of lipofuscin in cortisol-producing adenomas (CPAs) responsible for Cushing syndrome with and without the PRKACA (pLeu206Arg) somatic mutation, was investigated.
Mechanistically, Sirt1 (show SIRT1 Proteins) expression elevates phosphorylation of the alpha subunit (show POLG Proteins) of protein kinase A (PKA alpha), and this event is essential for Sirt1 (show SIRT1 Proteins)-induced phosphorylation of beta Catenin (show CTNNB1 Proteins).
Together, the results suggest a complex antagonistic interplay between the control of ARPP-16 (show ARPP19 Proteins) by MAST3 and PKA that creates a mechanism whereby cAMP mediates PP2A (show PPP2R4 Proteins) disinhibition.
CTR (show CALCR Proteins) activates AKAP2-anchored cAMP-dependent protein kinase A, which then phosphorylates tight junction proteins ZO-1 (show TJP1 Proteins) and claudin 3 (show CLDN3 Proteins).
These results indicate that Mixed fibrolamellar hepatocellular carcinoma (mFL-HCC (show FAM126A Proteins)) is similar to pure FL-HCC (show FAM126A Proteins) at the genomic level and the DNAJB1 (show DNAJB1 Proteins):PRKACA fusion can be used as a diagnostic tool for both pure and mFL-HCC (show FAM126A Proteins)
PRKACA mutations are highly specific for cortisol over-secretion, while they are absent or very rare in the context of other adrenal diseases. Patients carrying these somatic mutations are affected by a more severe phenotype and are identified at a younger age.
Somatic mutations in PRKACA, coding for the catalytic alpha subunit (show POLG Proteins) of protein kinase A (PKA), have been recently identified as the most frequent genetic alteration in cortisol-secreting adrenocortical adenomas, which are responsible for adrenal Cushing's syndrome.
PKA and MEK (thus, also pERK) are the intracellular mediators downstream of GPR30 that induce the non-genomic suppression of GnRH-induced LH secretion from bovine AP cells by estradiol or G1
Data indicate that mitochondrial cAMP-dependent protein kinase (PKA) activity is regulated by the protease calpain.
structural basis of selectivity for protein kinase A in complex with Rho-kinase (show ROCK1 Proteins) inhibitors by x-ray crystallography
Purification and characterisation of protein kinase catalytic subunit (PKAcat) from bovine lens.
ceramide as a potent physiological modulator of the Na(+)-ATPase, participating in a regulatory network in kidney cells and counteracting the stimulatory effect of PKA via PKCzeta (show PRKCZ Proteins)
we demonstrate that PKA, PKC (show FYN Proteins) and PI3K pathways crosstalk in porcine male germ cells to crucially regulate GSK3A (show GSK3a Proteins) phosphorylation which subsequently controls cell motility.
Study validates the DNAJB1 (show DNAJB1 Proteins)-PRKACA fusion kinase as an oncogenic driver and candidate drug target for fibrolamellar hepatocellular carcinoma in mouse model in which tumorigenesis was significantly enhanced by genetic activation of beta-catenin (show CTNNB1 Proteins).
Protein kinase A signaling explains vasopressin (show AVP Proteins)-mediated regulation of membrane trafficking and gene transcription.
Data suggest that the upregulation of mitochondrial respiratory chain proteins played a partial role in the protection of PKA/CREB (show CREB1 Proteins) signaling.
HIF1a (show HIF1A Proteins) transcriptional activity is stimulated by Protein kinase A-dependent phosphorylation
Generation of the Dnajb1 (show DNAJB1 Proteins)-Prkaca fusion gene in wild-type mice to be sufficient to initiate formation of tumors that have many features of human fibrolamellar hepatocellular carcinonma.
Data indicate a subpopulation of the CaV1.2 (show CACNA1C Proteins) channel pore-forming subunit (alpha1C) within nanometer proximity of protein kinase A (PKA) at the sarcolemma of murine and human arterial myocytes.
S1928A KI mice failed to induce long-term potentiation in response to prolonged theta-tetanus (PTT-LTP (show SCP2 Proteins)), a form of synaptic plasticity that requires Cav1.2 (show CACNA1C Proteins) and enhancement of its activity by the beta2-adrenergic receptor (show ADRB2 Proteins) (beta2AR (show ADRB2 Proteins))-cAMP-PKA cascade.
Data show that laminin alpha2beta1gamma1 (Lm211) can inhibit neuregulin 1 (show NRG1 Proteins) type III (Nrg1III) by limiting protein kinase A (PKA) activation, which is required to initiate myelination.
study identifies a new role of Dual-AKAP1 (show AKAP1 Proteins) in regulating mitochondrial trafficking through Miro-2 (show RHOT2 Proteins), and supports a model in which PINK1 (show PINK1 Proteins) and mitochondrial PKA participate in a similar neuroprotective signaling pathway to maintain dendrite connectivity
Data suggest that enzyme activation by cAMP involves highly stable conformation of Prkar1a as it binds to Prkaca; glycine residue, G235, appears to function as hinge in B/C helix conserved in Prkar1a; this "Flipback" conformation plays role in cAMP association to A domain of Prkar1a. (Prkar1a = cyclic AMP-dependent protein kinase RIalpha subunit; Prkaca = cyclic AMP-dependent protein kinase catalytic subunit)
support hypothesis that PRKACA activation is responsible for downstream protein tyrosine phosphorylation events in stallion sperm
Thus Ca(2 (show CA2 Proteins)+)-cAMP/PKA-dependent phosphorylation limits the rate and magnitude of increase in spontaneous action potential firing rate.
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. Alternatively spliced transcript variants encoding distinct isoforms have been observed.
, cAMP-dependent protein kinase catalytic subunit alpha
, protein kinase A catalytic subunit
, cAMP-dependent protein kinase catalytic subunit C alpha
, protein kinase A
, protein kinase, cAMP-dependent, catalytic, alpha
, C-alpha subunit
, sperm cAMP-dependent protein kinase catalytic subunit
, protein kinase A alpha
, PKA catalytic subunit alpha