scholarly journals Genes encoding catalytic subunits of protein kinase a and risk of spina bifida

2005 ◽  
Vol 73 (9) ◽  
pp. 591-596 ◽  
Author(s):  
Huiping Zhu ◽  
Wei Lu ◽  
Cecile Laurent ◽  
Gary M. Shaw ◽  
Edward J. Lammer ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Spina Bifida ◽  
Protein Kinase A ◽  
Catalytic Subunits ◽  
Genes Encoding ◽  
Kinase A

scholarly journals Protein Kinase A (PKA) Catalytic Subunits a and b Have Non‐Redundant Functions in Collecting Duct Cells

2020 ◽  
Vol 34 (S1) ◽  
pp. 1-1
Author(s):  
Karim Salhadar ◽  
V. Raghuram ◽  
Chin-Rang Yang ◽  
Kavee Limbutara ◽  
Mark Knepper
Keyword(s):  
Protein Kinase ◽  
Protein Kinase A ◽  
Collecting Duct ◽  
Catalytic Subunits ◽  
Duct Cells ◽  
Collecting Duct Cells ◽  
Redundant Functions ◽  
Kinase A

scholarly journals Protein kinase A translocation and insulin secretion in pancreatic β-cells: studies with adenylate cyclase toxin from Bordetella pertussis

2002 ◽  
Vol 368 (2) ◽  
pp. 397-404 ◽  
Author(s):  
Zhiyong GAO ◽  
Robert A. YOUNG ◽  
Matteo M. TRUCCO ◽  
Scott R. GREENE ◽  
Erik L. HEWLETT ◽  
...  
Keyword(s):  
Insulin Secretion ◽  
Protein Kinase ◽  
Adenylate Cyclase ◽  
Protein Kinase A ◽  
Dependent Protein Kinase ◽  
Catalytic Subunits ◽  
Dependent Protein ◽  
Adenylate Cyclase Toxin ◽  
Dose Dependent ◽  
Kinase A

Activation of protein kinase A (cAMP-dependent protein kinase; PKA) triggers insulin secretion in the β-cell. Adenylate cyclase toxin (ACT), a bacterial exotoxin with adenylate cyclase activity, and forskolin, an activator of adenylate cyclase, both dose-dependently increased insulin secretion in the presence, but not the absence, of glucose in insulin-secreting βTC3 cells. The stimulation of cAMP release by either agent was dose-dependent but glucose-independent. Omission of extracellular Ca2+ totally abolished the effects of ACT on insulin secretion and cytosolic cAMP accumulation. ACT and forskolin caused rapid and dramatic increases in cytosolic Ca2+, which were blocked by nifedipine and the omission of extracellular Ca2+. Omission of glucose completely blocked the effects of forskolin and partially blocked the effects of ACT on cytosolic Ca2+. PKA α, β and γ catalytic subunits (Cα, Cβ and Cγ respectively) were identified in βTC6 cells by confocal microscopy. Glucose and glucagon-like polypeptide-1 (GLP-1) caused translocation of Cα to the nucleus and of Cβ to the plasma membrane and the nucleus, but did not affect the distribution of Cγ. In conclusion, glucose and GLP-1 amplify insulin secretion via cAMP production and PKAβ activation.

scholarly journals Protein Kinase A Contributes to the Negative Control of Snf1 Protein Kinase in Saccharomyces cerevisiae

2011 ◽  
Vol 11 (2) ◽  
pp. 119-128 ◽  
Author(s):  
LaKisha Barrett ◽  
Marianna Orlova ◽  
Marcin Maziarz ◽  
Sergei Kuchin
Keyword(s):  
Protein Kinase ◽  
Protein Kinase A ◽  
Slow Growth ◽  
Negative Control ◽  
Regulatory Subunit ◽  
Checkpoint Control ◽  
Glucose Limitation ◽  
Genes Encoding ◽  
Kinase A

ABSTRACT Snf1 protein kinase regulates responses to glucose limitation and other stresses. Snf1 activation requires phosphorylation of its T-loop threonine by partially redundant upstream kinases (Sak1, Tos3, and Elm1). Under favorable conditions, Snf1 is turned off by Reg1-Glc7 protein phosphatase. The reg1 mutation causes increased Snf1 activation and slow growth. To identify new components of the Snf1 pathway, we searched for mutations that, like snf1 , suppress reg1 for the slow-growth phenotype. In addition to mutations in genes encoding known pathway components ( SNF1 , SNF4 , and SAK1 ), we recovered “fast” mutations, designated fst1 and fst2 . Unusual morphology of the mutants in the Σ1278b strains employed here helped us identify fst1 and fst2 as mutations in the RasGAP genes IRA1 and IRA2 . Cells lacking Ira1, Ira2, or Bcy1, the negative regulatory subunit of cyclic AMP (cAMP)-dependent protein kinase A (PKA), exhibited reduced Snf1 pathway activation. Conversely, Snf1 activation was elevated in cells lacking the Gpr1 sugar receptor, which contributes to PKA signaling. We show that the Snf1-activating kinase Sak1 is phosphorylated in vivo on a conserved serine (Ser1074) within an ideal PKA motif. However, this phosphorylation alone appears to play only a modest role in regulation, and Sak1 is not the only relevant target of the PKA pathway. Collectively, our results suggest that PKA, which integrates multiple regulatory inputs, could contribute to Snf1 regulation under various conditions via a complex mechanism. Our results also support the view that, like its mammalian counterpart, AMP-activated protein kinase (AMPK), yeast Snf1 participates in metabolic checkpoint control that coordinates growth with nutrient availability.

Protein kinase a in postmortem brain of depressed suicide victims: altered expression of specific regulatory and catalytic subunits

2004 ◽  
Vol 55 (3) ◽  
pp. 234-243 ◽  
Author(s):  
Yogesh Dwivedi ◽  
Hooriyah S Rizavi ◽  
Pradeep K Shukla ◽  
Jennifer Lyons ◽  
Gabor Faludi ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Protein Kinase A ◽  
Postmortem Brain ◽  
Altered Expression ◽  
Catalytic Subunits ◽  
Kinase A

scholarly journals Protein Kinase A Regulates MYC Protein through Transcriptional and Post-translational Mechanisms in a Catalytic Subunit Isoform-specific Manner

2013 ◽  
Vol 288 (20) ◽  
pp. 14158-14169 ◽  
Author(s):  
Achuth Padmanabhan ◽  
Xiang Li ◽  
Charles J. Bieberich
Keyword(s):  
Protein Kinase ◽  
Protein Kinase A ◽  
Term Effect ◽  
Catalytic Subunit ◽  
Short Term ◽  
Catalytic Subunits ◽  
Multiple Substrates ◽  
Pka Catalytic Subunit ◽  
Kinase A ◽  
In Cells

MYC levels are tightly regulated in cells, and deregulation is associated with many cancers. In this report, we describe the existence of a MYC-protein kinase A (PKA)-polo-like kinase 1 (PLK1) signaling loop in cells. We report that sequential MYC phosphorylation by PKA and PLK1 protects MYC from proteasome-mediated degradation. Interestingly, short term pan-PKA inhibition diminishes MYC level, whereas prolonged PKA catalytic subunit α (PKACα) knockdown, but not PKA catalytic subunit β (PKACβ) knockdown, increases MYC. We show that the short term effect of pan-PKA inhibition on MYC is post-translational and the PKACα-specific long term effect on MYC is transcriptional. These data also reveal distinct functional roles among PKA catalytic isoforms in MYC regulation. We attribute this effect to differential phosphorylation selectivity among PKA catalytic subunits, which we demonstrate for multiple substrates. Further, we also show that MYC up-regulates PKACβ, transcriptionally forming a proximate positive feedback loop. These results establish PKA as a regulator of MYC and highlight the distinct biological roles of the different PKA catalytic subunits.

scholarly journals CNOT1 mediates phosphorylation via Protein kinase A on the circadian clock

2019 ◽  
Author(s):  
Yunfeng Zhang ◽  
Haitang Qin ◽  
Yongjie Feng ◽  
Peng Gao ◽  
Yingbin Zhong ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Circadian Clock ◽  
Protein Kinase A ◽  
Feedback Loop ◽  
Critical Role ◽  
Positive Element ◽  
Endogenous Protein ◽  
Genes Encoding ◽  
Genetic Deletion ◽  
Kinase A

AbstractAt the core of the mammalian circadian feedback loop, CLOCK (NPAS2)-BMAL1 is the positive element to activate transcription of downstream genes encoding the negative elements PERs and CRYs. Here we show that CNOT1 associates with both CLOCK and BMAL1, promotes their phosphorylation and increases their protein stability, and in turn inhibits the transcriptional activity of CLOCK-BMAL1. Expression of either CLOCK, BMAL1 or CNOT1 could interact with endogenous Protein Kinase A (PKA) as assessed by co-immunoprecipitation (Co-IP) and kinase assays. PKA could phosphorylate CLOCK and BMAL1 and this was promoted by CNOT1. Genetic deletion of PKA-Cα by CRISPR-Cas9 results in a longer period of the circadian rhythm; while overexpression of PKA-Cα induces a shorter period. Furthermore, we demonstrate that CNOT1 associates with CLOCK and BMAL1 in the mouse liver and promotes their phosphorylation. PER2, but not CRY2, is also a PKA target. Our results suggest that CNOT1 and PKA play a critical role in the mammalian circadian clock, revealing a conserved function in eukaryotic circadian regulations.

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