β2-Adrenergic Receptor Lacking the Cyclic AMP-Dependent Protein Kinase Consensus Sites Fully Activates Extracellular Signal-Regulated Kinase 1/2 in Human Embryonic Kidney 293 Cells: Lack of Evidence for Gs/GiSwitching.

2002 ◽  
Vol 62 (5) ◽  
pp. 1094-1102 ◽  
Author(s):  
Jacqueline Friedman ◽  
Bonita Babu ◽  
Richard B. Clark
Keyword(s):  
Protein Kinase ◽  
Cyclic Amp ◽  
Adrenergic Receptor ◽  
Human Embryonic Kidney ◽  
Dependent Protein Kinase ◽  
Extracellular Signal Regulated Kinase ◽  
293 Cells ◽  
Extracellular Signal ◽  
Dependent Protein ◽  
Β2 Adrenergic Receptor

scholarly journals Palmitoylated Cysteine 341 Modulates Phosphorylation of the β2-Adrenergic Receptor by the cAMP-dependent Protein Kinase

1996 ◽  
Vol 271 (35) ◽  
pp. 21490-21497 ◽  
Author(s):  
Serge Moffett ◽  
Lynda Adam ◽  
Hélène Bonin ◽  
Thomas P. Loisel ◽  
Michel Bouvier ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Adrenergic Receptor ◽  
Dependent Protein Kinase ◽  
Camp Dependent Protein Kinase ◽  
Dependent Protein ◽  
Β2 Adrenergic Receptor

Evidence for the involvement of CaMKII and AMPK in Ca2+-dependent signaling pathways regulating FA uptake and oxidation in contracting rodent muscle

2008 ◽  
Vol 104 (5) ◽  
pp. 1366-1373 ◽  
Author(s):  
Marcella A. Raney ◽  
Lorraine P. Turcotte
Keyword(s):  
Electrical Stimulation ◽  
Protein Kinase ◽  
Dependent Protein Kinase ◽  
Extracellular Signal Regulated Kinase ◽  
Calcium Calmodulin Dependent ◽  
Extracellular Signal ◽  
Regulation Of Contraction ◽  
Dependent Protein ◽  
Ampk Activity ◽  
Amp Activated Protein Kinase

Calcium-calmodulin/dependent protein kinase II (CaMKII), AMP-activated protein kinase (AMPK), and extracellular signal-regulated kinase (ERK1/2) have each been implicated in the regulation of substrate metabolism during exercise. The purpose of this study was to determine whether CaMKII is involved in the regulation of FA uptake and oxidation and, if it is involved, whether it does so independently of AMPK and ERK1/2. Rat hindquarters were perfused at rest with ( n = 16) or without ( n = 10) 3 mM caffeine, or during electrical stimulation ( n = 14). For each condition, rats were subdivided and treated with 10 μM of either KN92 or KN93, inactive and active CaMKII inhibitors, respectively. Both caffeine treatment and electrical stimulation significantly increased FA uptake and oxidation. KN93 abolished caffeine-induced FA uptake, decreased contraction-induced FA uptake by 33%, and abolished both caffeine- and contraction-induced FA oxidation ( P < 0.05). Caffeine had no effect on ERK1/2 phosphorylation ( P > 0.05) and increased α2-AMPK activity by 68% ( P < 0.05). Electrical stimulation increased ERK1/2 phosphorylation and α2-AMPK activity by 51% and 3.4-fold, respectively ( P < 0.05). KN93 had no effect on caffeine-induced α2-AMPK activity, ERK1/2 phosphorylation, or contraction-induced ERK1/2 phosphorylation ( P > 0.05). Alternatively, it decreased contraction-induced α2-AMPK activity by 51% ( P < 0.05), suggesting that CaMKII lies upstream of AMPK. These results demonstrate that regulation of contraction-induced FA uptake and oxidation occurs in part via Ca2+-independent activation of ERK1/2 as well as Ca2+-dependent activation of CaMKII and AMPK.

scholarly journals Role of the Cyclic AMP-dependent Protein Kinase in Homologous Resensitization of the β1-Adrenergic Receptor

2004 ◽  
Vol 279 (20) ◽  
pp. 21135-21143 ◽  
Author(s):  
Lidia A. Gardner ◽  
Noel M. Delos Santos ◽  
Shannon G. Matta ◽  
Michael A. Whitt ◽  
Suleiman W. Bahouth
Keyword(s):  
Protein Kinase ◽  
Cyclic Amp ◽  
Adrenergic Receptor ◽  
Dependent Protein Kinase ◽  
Dependent Protein

scholarly journals AKAP79-mediated Targeting of the Cyclic AMP-dependent Protein Kinase to the β1-Adrenergic Receptor Promotes Recycling and Functional Resensitization of the Receptor

2006 ◽  
Vol 281 (44) ◽  
pp. 33537-33553 ◽  
Author(s):  
Lidia A. Gardner ◽  
Steven J. Tavalin ◽  
April S. Goehring ◽  
John D. Scott ◽  
Suleiman W. Bahouth
Keyword(s):  
Protein Kinase ◽  
Cyclic Amp ◽  
Adrenergic Receptor ◽  
Dependent Protein Kinase ◽  
Dependent Protein

scholarly journals Cyclic AMP-Dependent Kinase Regulates Raf-1 Kinase Mainly by Phosphorylation of Serine 259

2002 ◽  
Vol 22 (10) ◽  
pp. 3237-3246 ◽  
Author(s):  
Amardeep S. Dhillon ◽  
Claire Pollock ◽  
Helge Steen ◽  
Peter E. Shaw ◽  
Harald Mischak ◽  
...  
Keyword(s):  
Cyclic Amp ◽  
Kinase Activity ◽  
Dependent Manner ◽  
Dependent Protein Kinase ◽  
Extracellular Signal Regulated Kinase ◽  
Extracellular Signal ◽  
Dependent Protein ◽  
Kinase Pathway

ABSTRACT The Raf-1 kinase activates the ERK (extracellular-signal-regulated kinase) pathway. The cyclic AMP (cAMP)-dependent protein kinase (PKA) can inhibit Raf-1 by direct phosphorylation. We have mapped all cAMP-induced phosphorylation sites in Raf-1, showing that serines 43, 259, and 621 are phosphorylated by PKA in vitro and induced by cAMP in vivo. Serine 43 phosphorylation decreased the binding to Ras in serum-starved but not in mitogen-stimulated cells. However, the kinase activity of a RafS43A mutant was fully inhibited by PKA. Mutation of serine 259 increased the basal Raf-1 activity and rendered it largely resistant to inhibition by PKA. cAMP increased Raf-1 serine 259 phosphorylation in a PKA-dependent manner with kinetics that correlated with ERK deactivation. PKA also decreased Raf-1 serine 338 phosphorylation of Raf-1, previously shown to be required for Raf-1 activation. Serine 338 phosphorylation of a RafS259A mutant was unaffected by PKA. Using RafS259 mutants we also demonstrate that Raf-1 is the sole target for PKA inhibition of ERK and ERK-induced gene expression, and that Raf-1 inhibition is mediated mainly through serine 259 phosphorylation.

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