Browse our Protein Kinase, CAMP-Dependent, Regulatory, Type I, alpha (Tissue Specific Extinguisher 1) Proteins (PRKAR1A)

Human Protein Kinase, CAMP-Dependent, Regulatory, Type I, alpha (Tissue Specific Extinguisher 1) (PRKAR1A) interaction partners

1. the T allele of SNP rs60684937 located at 67,419,130 bp on chromosome 17 was associated with increased plasma EPO (show EPO Proteins) and a relatively increased expression of a non-coding transcript of PRKAR1A in sickle cell disease patients

2. In this study we demonstrate a new role of MRAP2 in the regulation of the orexin receptor 1 (OX1R (show HCRTR1 Proteins)) and identify the specific regions of MRAP2 required for the regulation of OX1R (show HCRTR1 Proteins) and PKR1 (show PROKR1 Proteins). Importantly, like MC4R (show MC4R Proteins) and PKRs, OX1R (show HCRTR1 Proteins) is predominately expressed in the brain where it regulates food intake

3. Screening of PRKAR1A and PDE4D (show PDE4D Proteins) in a Large Italian Series of Patients Clinically Diagnosed With Albright Hereditary Osteodystrophy and/or Pseudohypoparathyroidism

4. Found evidence for kidney and liver cystic phenotypes in the Carney complex, a tumoral syndrome caused by mut (show PKD1 Proteins)ations in PRKAR1A.

5. Data suggest that introduction of cGMP-specific (show PDE6A Proteins) 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.

6. Data show that ELOVL7, SOCS3 (show SOCS3 Proteins), ACSL4 (show ACSL4 Proteins) and CLU (show CLU Proteins) were upregulated while PRKAR1A and ABCG1 (show ABCG1 Proteins) were downregulated in the phlegm-dampness group.

7. Electrostatic interactions are mediators in the allosteric activation of protein kinase A RIalpha.

8. 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.

9. This study reports a novel point mutation of the PRKAR1A gene in a patient with Carney complex who presented with significant osteoporosis and fractures.

10. Letter/Case Report: novel PRKAR1A mutation resulting in a splicing variant in a case of Carney complex.

Mouse (Murine) Protein Kinase, CAMP-Dependent, Regulatory, Type I, alpha (Tissue Specific Extinguisher 1) (PRKAR1A) interaction partners

1. 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.

2. 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.

3. This study demonstrated that loss of one Prkar1a allele was associated with a significant increase in PKA activity in the basolateral (BLA (show LACTB Proteins)) and central (CeA (show CEA Proteins)) amygdala and ventromedial hypothalamus (VMH) in both Prkar1a(+/-) and Prkar1a(+/-)/Prkaca (show PRKACA Proteins)(+/-) mice.

4. Kidney-specific loss of Prkar1a induced renal cystic disease and markedly aggravated cystogenesis in the Pkd1 (show PKD1 Proteins)(RC) models.

5. data demonstrate that haploinsufficiency for either one of the type-II regulatory subunits improved the bone phenotype of mice haploinsufficient for Prkar1a

6. 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.

7. Prkar1a activation enhances beta-catenin (show CTNNB1 Proteins) transcriptional activity through nuclear localization to PML (show PML Proteins) bodies.

8. Loss of Prkar1a can only promote tumorigenesis when Prkar1a-mediated apoptosis is somehow countered.

9. Data show that mammary-specific loss of Prkar1a leads to elevated type-II PKA isozyme activation and this is sufficient to drive breast carcinogenesis.

10. Results show that mouse Prkar1a and human PRKAR2A (show PRKAR2A Proteins) exhibited a dynamic spatio-temporal expression in tooth development, whereas neither human PRKAR1A nor mouse Prkar2a (show PRKAR2A Proteins) showed their expression in odontogenesis.

Pig (Porcine) Protein Kinase, CAMP-Dependent, Regulatory, Type I, alpha (Tissue Specific Extinguisher 1) (PRKAR1A) interaction partners

1. ceramide activates plasma membrane Ca2+-ATPase from kidney-promixal tubule cells with protein kinase A as an intermediate

Zebrafish Protein Kinase, CAMP-Dependent, Regulatory, Type I, alpha (Tissue Specific Extinguisher 1) (PRKAR1A) interaction partners

1. Results demonstrate that PKA activity regulated by Mys is indispensable for negative regulation of the Hh signaling pathway in Hh-responsive cells.

Cow (Bovine) Protein Kinase, CAMP-Dependent, Regulatory, Type I, alpha (Tissue Specific Extinguisher 1) (PRKAR1A) interaction partners

1. 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)

2. Data suggest PRKAR1A contains two structurally homologous cAMP-binding domains that exhibit marked differences in dynamic profiles in activation/inhibition of Prkaca (show PRKACA Proteins); conservation of structure does not necessarily imply conservation of dynamics.

3. Results describe the structures of the protein kinase A RIalpha subunit D/D domain alone and in complex with D-AKAP2 (show AKAP10 Proteins).

4. Data show that RSK1 (show RPS6KA1 Proteins) regulates PKAc activity in a cAMP-independent manner, and PKARIalpha by associating with RSK1 (show RPS6KA1 Proteins) regulates its activation and its biological functions.

5. angle X-ray scattering studies indicate RIalpha, RIIalpha, and RIIbeta (show PRKAR2B Proteins) homodimers differ markedly in overall shape despite extensive sequence homology and similar molecular masses;cAMP binding does not cause large conformational changes(Prkar1a, Prkar2a (show PRKAR2A Proteins))

6. the PKA RIalpha subunit dynamic C helix mediates isoform-specific domain reorganization upon C subunit binding