scholarly journals β1‐Adrenergic receptor signaling activates TRPV5 via the protein kinase A pathway (1181.4)

2014 ◽  
Vol 28 (S1) ◽  
Author(s):  
Joost Hoenderop ◽  
Eline Hagen ◽  
Kukiat Tudpor ◽  
Sjoerd Verkaart ◽  
Rene Bindels
Keyword(s):  
Protein Kinase ◽  
Protein Kinase A ◽  
Adrenergic Receptor ◽  
Receptor Signaling ◽  
Kinase A

scholarly journals Gravin Orchestrates Protein Kinase A and  2-Adrenergic Receptor Signaling Critical for Synaptic Plasticity and Memory

2012 ◽  
Vol 32 (50) ◽  
pp. 18137-18149 ◽  
Author(s):  
R. Havekes ◽  
D. A. Canton ◽  
A. J. Park ◽  
T. Huang ◽  
T. Nie ◽  
...  
Keyword(s):  
Synaptic Plasticity ◽  
Protein Kinase ◽  
Protein Kinase A ◽  
Adrenergic Receptor ◽  
Receptor Signaling ◽  
Kinase A

Identification of a Gs activator region of the β2-adrenergic receptor that is autoregulated via protein kinase A-dependent phosphorylation

Cell ◽  
1991 ◽  
Vol 67 (4) ◽  
pp. 723-730 ◽  
Author(s):  
Takashi Okamoto ◽  
Yoshitake Murayama ◽  
Yujiro Hayashi ◽  
Masaki Inagaki ◽  
Etsuro Ogata ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Protein Kinase A ◽  
Adrenergic Receptor ◽  
Β2 Adrenergic Receptor ◽  
Kinase A

scholarly journals Distinct Protein Kinase A Anchoring Proteins Direct Prostaglandin E2Modulation of Toll-like Receptor Signaling in Alveolar Macrophages

2011 ◽  
Vol 286 (11) ◽  
pp. 8875-8883 ◽  
Author(s):  
Sang-Hoon Kim ◽  
Carlos Henrique Serezani ◽  
Katsuhide Okunishi ◽  
Zbigniew Zaslona ◽  
David M. Aronoff ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Protein Kinase A ◽  
Alveolar Macrophages ◽  
Receptor Signaling ◽  
Toll Like Receptor ◽  
Anchoring Proteins ◽  
Kinase A

scholarly journals β2-Adrenergic Receptor-induced p38 MAPK Activation Is Mediated by Protein Kinase A Rather than by Gior Gβγ in Adult Mouse Cardiomyocytes

2000 ◽  
Vol 275 (51) ◽  
pp. 40635-40640 ◽  
Author(s):  
Ming Zheng ◽  
Sheng-Jun Zhang ◽  
Wei-Zhong Zhu ◽  
Bruce Ziman ◽  
Brian K. Kobilka ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Protein Kinase A ◽  
P38 Mapk ◽  
Adrenergic Receptor ◽  
Adult Mouse ◽  
Mapk Activation ◽  
Β2 Adrenergic Receptor ◽  
Kinase A

scholarly journals Regulation of Cardiac L-Type Ca 2+ Channel Ca V 1.2 Via the β-Adrenergic-cAMP-Protein Kinase A Pathway

2013 ◽  
Vol 113 (5) ◽  
pp. 617-631 ◽  
Author(s):  
Sharon Weiss ◽  
Shimrit Oz ◽  
Adva Benmocha ◽  
Nathan Dascal
Keyword(s):  
Protein Kinase ◽  
Protein Kinase A ◽  
Adrenergic Receptor ◽  
Transgenic Animals ◽  
Receptor Activation ◽  
Model Systems ◽  
Adrenergic Stimulation ◽  
New Findings ◽  
Kinase A

In the heart, adrenergic stimulation activates the β-adrenergic receptors coupled to the heterotrimeric stimulatory G s protein, followed by subsequent activation of adenylyl cyclase, elevation of cyclic AMP levels, and protein kinase A (PKA) activation. One of the main targets for PKA modulation is the cardiac L-type Ca 2+ channel (Ca V 1.2) located in the plasma membrane and along the T-tubules, which mediates Ca 2+ entry into cardiomyocytes. β-Adrenergic receptor activation increases the Ca 2+ current via Ca V 1.2 channels and is responsible for the positive ionotropic effect of adrenergic stimulation. Despite decades of research, the molecular mechanism underlying this modulation has not been fully resolved. On the contrary, initial reports of identification of key components in this modulation were later refuted using advanced model systems, especially transgenic animals. Some of the cardinal debated issues include details of specific subunits and residues in Ca V 1.2 phosphorylated by PKA, the nature, extent, and role of post-translational processing of Ca V 1.2, and the role of auxiliary proteins (such as A kinase anchoring proteins) involved in PKA regulation. In addition, the previously proposed crucial role of PKA in modulation of unstimulated Ca 2+ current in the absence of β-adrenergic receptor stimulation and in voltage-dependent facilitation of Ca V 1.2 remains uncertain. Full reconstitution of the β-adrenergic receptor signaling pathway in heterologous expression systems remains an unmet challenge. This review summarizes the past and new findings, the mechanisms proposed and later proven, rejected or disputed, and emphasizes the essential issues that remain unresolved.

scholarly journals Protein Kinase A Phosphorylation of Spinophilin Modulates Its Interaction with the α2A-Adrenergic Receptor (AR) and Alters Temporal Properties of α2AAR Internalization

2008 ◽  
Vol 283 (21) ◽  
pp. 14516-14523 ◽  
Author(s):  
Jianmin Xu ◽  
Yunjia Chen ◽  
Roujian Lu ◽  
Christopher Cottingham ◽  
Kai Jiao ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Protein Kinase A ◽  
Adrenergic Receptor ◽  
Temporal Properties ◽  
Kinase A
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