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In this study we demonstrate a new role of MRAP2 in the regulation of the orexin receptor 1 (OX1R (zeige HCRTR1 Proteine)) and identify the specific regions of MRAP2 required for the regulation of OX1R (zeige HCRTR1 Proteine) and PKR1 (zeige PROKR1 Proteine). Importantly, like MC4R (zeige MC4R Proteine) and PKRs, OX1R (zeige HCRTR1 Proteine) is predominately expressed in the brain where it regulates food intake
Screening of PRKAR1A and PDE4D (zeige PDE4D Proteine) in a Large Italian Series of Patients Clinically Diagnosed With Albright Hereditary Osteodystrophy and/or Pseudohypoparathyroidism
Found evidence for kidney and liver cystic phenotypes in the Carney complex, a tumoral syndrome caused by mut (zeige PKD1 Proteine)ations in PRKAR1A.
Data suggest that introduction of cGMP-specific (zeige PDE6A Proteine) residues using site-directed mutagenesis reduces selectivity of cyclic nucleotide-binding domain (CNBD) of PRKAR1A; combination of two mutations (G316R/A336T) results in a cGMP-selective binding site in the C-terminal CNBD; introduction of corresponding mutations (T192R/A212T) into the N-terminal CNBD results in a highly cGMP-selective binding site.
Data show that ELOVL7, SOCS3 (zeige SOCS3 Proteine), ACSL4 (zeige ACSL4 Proteine) and CLU (zeige CLU Proteine) were upregulated while PRKAR1A and ABCG1 (zeige ABCG1 Proteine) were downregulated in the phlegm-dampness group.
Electrostatic interactions are mediators in the allosteric activation of protein kinase A RIalpha.
the present study reported for the first time an intronic splice site mutation in the PRKAR1A gene of a Chinese family with Carney complex, which probably caused skin pigmentation observed in affected family members.
This study reports a novel point mutation of the PRKAR1A gene in a patient with Carney complex who presented with significant osteoporosis and fractures.
Letter/Case Report: novel PRKAR1A mutation resulting in a splicing variant in a case of Carney complex.
P-Rex1 contributes to the spatiotemporal localization of type I PKA, which tightly regulates this guanine exchange factor by a multistep mechanism.
This mouse knockout model supports the role of prkar1a as a tumor suppressor gene in the pancreas and points to the PKA pathway as a possible therapeutic target for these lesions.
This model, the first describing the germline expression of a PRKAR1A mutation causing dominant repression of cAMP-dependent PKA, reproduced the main features of acrodysostosis 1 in humans.
This study demonstrated that loss of one Prkar1a allele was associated with a significant increase in PKA activity in the basolateral (BLA (zeige LACTB Proteine)) and central (CeA (zeige CEA Proteine)) amygdala and ventromedial hypothalamus (VMH) in both Prkar1a(+/-) and Prkar1a(+/-)/Prkaca (zeige PRKACA Proteine)(+/-) mice.
Kidney-specific loss of Prkar1a induced renal cystic disease and markedly aggravated cystogenesis in the Pkd1 (zeige PKD1 Proteine)(RC) models.
data demonstrate that haploinsufficiency for either one of the type-II regulatory subunits improved the bone phenotype of mice haploinsufficient for Prkar1a
PRKAR1A gene and its locus are altered in mixed odontogenic tumors. Expression is decreased in a subset of tumors, and Prkar1a(+) (/) (-) mice do not show abnormalities, which indicates that additional genes play a role in this tumor's pathogenesis.
Prkar1a activation enhances beta-catenin (zeige CTNNB1 Proteine) transcriptional activity through nuclear localization to PML (zeige PML Proteine) bodies.
Loss of Prkar1a can only promote tumorigenesis when Prkar1a-mediated apoptosis is somehow countered.
Data show that mammary-specific loss of Prkar1a leads to elevated type-II PKA isozyme activation and this is sufficient to drive breast carcinogenesis.
Results show that mouse Prkar1a and human PRKAR2A (zeige PRKAR2A Proteine) exhibited a dynamic spatio-temporal expression in tooth development, whereas neither human PRKAR1A nor mouse Prkar2a (zeige PRKAR2A Proteine) showed their expression in odontogenesis.
ceramide activates plasma membrane Ca2+-ATPase from kidney-promixal tubule cells with protein kinase A as an intermediate
Results demonstrate that PKA activity regulated by Mys is indispensable for negative regulation of the Hh signaling pathway in Hh-responsive cells.
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)
Data suggest PRKAR1A contains two structurally homologous cAMP-binding domains that exhibit marked differences in dynamic profiles in activation/inhibition of Prkaca (zeige PRKACA Proteine); conservation of structure does not necessarily imply conservation of dynamics.
Results describe the structures of the protein kinase A RIalpha subunit D/D domain alone and in complex with D-AKAP2 (zeige AKAP10 Proteine).
Data show that RSK1 (zeige RPS6KA1 Proteine) regulates PKAc activity in a cAMP-independent manner, and PKARIalpha by associating with RSK1 (zeige RPS6KA1 Proteine) regulates its activation and its biological functions.
angle X-ray scattering studies indicate RIalpha, RIIalpha, and RIIbeta (zeige PRKAR2B Proteine) homodimers differ markedly in overall shape despite extensive sequence homology and similar molecular masses;cAMP binding does not cause large conformational changes(Prkar1a, Prkar2a (zeige PRKAR2A Proteine))
the PKA RIalpha subunit dynamic C helix mediates isoform-specific domain reorganization upon C subunit binding
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. This gene encodes one of the regulatory subunits. This protein was found to be a tissue-specific extinguisher that down-regulates the expression of seven liver genes in hepatoma x fibroblast hybrids. Mutations in this gene cause Carney complex (CNC). This gene can fuse to the RET protooncogene by gene rearrangement and form the thyroid tumor-specific chimeric oncogene known as PTC2. A nonconventional nuclear localization sequence (NLS) has been found for this protein which suggests a role in DNA replication via the protein serving as a nuclear transport protein for the second subunit of the Replication Factor C (RFC40). Several alternatively spliced transcript variants encoding two different isoforms have been observed.
cAMP-dependent protein kinase regulatory subunit RIalpha
, cAMP-dependent protein kinase type I-alpha regulatory chain
, cAMP-dependent protein kinase type I-alpha regulatory subunit
, protein kinase A type 1a regulatory subunit
, tissue-specific extinguisher 1
, protein kinase, cAMP dependent regulatory, type 1, alpha
, protein kinase, cAMP dependent regulatory, type I, alpha
, cAMP-dependent protein kinase type I regulatory subunit
, protein kinase, cAMP-dependent, regulatory, type I, alpha (tissue specific extinguisher 1)
, cAMP-dependent protein kinase, regulatory subunit alpha 1
, cAMP-dependent protein kinase regulatory subunit alpha 1
, cAMP-dependent protein kinase type I-alpha regulatory subunit-like
, protein kinase, cAMP-dependent, regulatory subunit type I alpha S homeolog