scholarly journals Wnt signaling and PKA control Nodal expression and left-right determination in the chick embryo

Development ◽  
2001 ◽  
Vol 128 (16) ◽  
pp. 3189-3195 ◽  
Author(s):  
Concepción Rodríguez-Esteban ◽  
Javier Capdevila ◽  
Yasuhiko Kawakami ◽  
Juan Carlos Izpisúa Belmonte
Keyword(s):  
Protein Kinase ◽  
Chick Embryo ◽  
Wnt Signaling ◽  
Protein Kinase A ◽  
Adhesion Protein ◽  
Fibroblast Growth Factor 8 ◽  
Endogenous Protein ◽  
Asymmetric Pattern ◽  
The Right ◽  
Kinase A

Expression of the Nodal gene, which encodes a member of the TGFβ superfamily of secreted factors, localizes to the left side of the developing embryo in all vertebrates examined so far. This asymmetric pattern correlates with normal development of the left-right axis. We now show that the Wnt and PKA signaling pathways control left-right determination in the chick embryo through Nodal. A Wnt/β-catenin pathway controlsNodal expression in and around Hensen's node, without affecting the upstream regulators Sonic hedgehog, Car and Fibroblast Growth Factor 8. Transcription of Nodal is also positively regulated by a protein kinase A-dependent pathway. Both the adhesion protein N-cadherin and PKI (an endogenous protein kinase A inhibitor) are localized to the right side of the node and may contribute to restrict Nodal activation by Wnt signaling and PKA to the left side of the node.

Endogenous protein kinase A inhibitor (PKI?) modulates synaptic activity

1998 ◽  
Vol 53 (3) ◽  
pp. 269-278 ◽  
Author(s):  
Luis de Lecea ◽  
Jos� R. Criado ◽  
Santiago Rivera ◽  
Wei Wen ◽  
Eduardo Soriano ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Protein Kinase A ◽  
Synaptic Activity ◽  
Endogenous Protein ◽  
Kinase A

scholarly journals Protein kinase A-dependent increase in WAVE2 expression induced by the focal adhesion protein vinexin

2006 ◽  
Vol 11 (3) ◽  
pp. 281-292 ◽  
Author(s):  
Masaru Mitsushima ◽  
Takuhito Sezaki ◽  
Rie Akahane ◽  
Kazumitsu Ueda ◽  
Shiro Suetsugu ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Protein Kinase A ◽  
Focal Adhesion ◽  
Adhesion Protein ◽  
Focal Adhesion Protein ◽  
Kinase A

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.

Activation of KCa channels in airway smooth muscle cells by endogenous protein kinase A

1996 ◽  
Vol 271 (1) ◽  
pp. L100-L105 ◽  
Author(s):  
Z. W. Wang ◽  
M. I. Kotlikoff
Keyword(s):  
Protein Kinase ◽  
Protein Kinase A ◽  
Airway Smooth Muscle Cells ◽  
Channel Activity ◽  
Inhibitory Peptide ◽  
Kca Channels ◽  
Anchoring Proteins ◽  
Endogenous Protein ◽  
Gamma S ◽  
Kinase A

The regulation of calcium-activated potassium (KCa) channels by endogenous protein kinase A (PKA) was examined in inside-out patches from equine tracheal myocytes. In the absence of exogenous protein kinases, ATP (500 microM) significantly augmented KCa channel activity when applied to the cytosolic patch surface [open-state probability (nP0, mean +/- SE) increased from 0.010 +/- 0.001 to 0.034 +/- 0.005 (n = 24)]. The stimulatory effect of ATP was mimicked by ATP-gamma-S but not by AMP-PNP. Rather, AMP-PNP significantly inhibited channel activity. The PKA inhibitory peptide (PKI) significantly reduced nPo and prevented the augmenting effect of subsequent ATP. Ht 31, an inhibitory peptide for A-kinase-anchoring proteins (AKAP), but not its proline-substituted mutant, also blocked the stimulatory effect of ATP. These results suggest that 1) ATP augments KCa channel activity through phosphorylation; 2) the phosphorylation is catalyzed by endogenous PKA; 3) anchoring via AKAP is required to maintain association of PKA with the membrane; and 4) in a newly obtained patch, some of the KCa channels are probably already in a phosphorylated state.

scholarly journals Polarized Sphingolipid Transport from the Subapical Compartment Changes during Cell Polarity Development

2000 ◽  
Vol 11 (3) ◽  
pp. 1093-1101 ◽  
Author(s):  
Sven C.D. van IJzendoorn ◽  
Dick Hoekstra
Keyword(s):  
Protein Kinase ◽  
Protein Kinase A ◽  
Transport Pathway ◽  
Transient Activation ◽  
Endogenous Protein ◽  
Polarized Transport ◽  
Recycling Pathway ◽  
Specific Membrane ◽  
Kinase A ◽  
Fluorescent Analogues

The subapical compartment (SAC) plays an important role in the polarized transport of proteins and lipids. In hepatoma-derived HepG2 cells, fluorescent analogues of sphingomyelin and glucosylceramide are sorted in the SAC. Here, evidence is provided that shows that polarity development is regulated by a transient activation of endogenous protein kinase A and involves a transient activation of a specific membrane transport pathway, marked by the trafficking of the labeled sphingomyelin, from the SAC to the apical membrane. This protein kinase A–regulated pathway differs from the apical recycling pathway, which also traverses SAC. After reaching optimal polarity, the direction of the apically activated pathway switches to one in the basolateral direction, without affecting the apical recycling pathway.

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