scholarly journals Activated G Protein-coupled Receptor Induces Tyrosine Phosphorylation of STAT3 and Agonist-selective Serine Phosphorylation via Sustained Stimulation of Mitogen-activated Protein Kinase

1999 ◽  
Vol 274 (23) ◽  
pp. 16423-16430 ◽  
Author(s):  
Lynda A. Sellers ◽  
Wasyl Feniuk ◽  
Patrick P. A. Humphrey ◽  
Heather Lauder
Keyword(s):  
Protein Kinase ◽  
Tyrosine Phosphorylation ◽  
G Protein ◽  
Serine Phosphorylation ◽  
Mitogen Activated Protein Kinase ◽  
G Protein Coupled Receptor ◽  
Mitogen Activated Protein ◽  
G Protein Coupled ◽  
Stimulation Of

scholarly journals G Protein-Coupled Receptor-Mediated Mitogen-Activated Protein Kinase Activation through Cooperation of Gαq and Gαi Signals

2000 ◽  
Vol 20 (18) ◽  
pp. 6837-6848 ◽  
Author(s):  
Andree Blaukat ◽  
Ana Barac ◽  
Michael J. Cross ◽  
Stefan Offermanns ◽  
Ivan Dikic
Keyword(s):  
Protein Kinase ◽  
G Protein ◽  
Tyrosine Kinases ◽  
Synergistic Effects ◽  
Mitogen Activated Protein Kinase ◽  
General Mechanism ◽  
Mitogen Activated Protein ◽  
Novel Concept ◽  
G Protein Coupled ◽  
Stimulation Of

ABSTRACT G protein-coupled receptors (GPCRs) have been shown to stimulate extracellular regulated kinases (ERKs) through a number of linear pathways that are initiated by Gq/11 or Giproteins. We studied signaling to the ERK cascade by receptors that simultaneously activate both G protein subfamilies. In HEK293T cells, bradykinin B2 receptor (B2R)-induced stimulation of ERK2 and transcriptional activity of Elk1 are dependent on Gαq-mediated protein kinase C (PKC) and on Gαi-induced Ras activation, while they are independent of Gβγ subunits, phosphatidylinositol 3-kinase, and tyrosine kinases. Similar results were obtained with m1 and m3muscarinic receptors in HEK293T cells and with the B2R in human and mouse fibroblasts, indicating a general mechanism in signaling toward the ERK cascade. Furthermore, the bradykinin-induced activation of ERK is strongly reduced in Gαq/11-deficient fibroblasts. In addition, we found that constitutively active mutants of Gαq/11 or Gαi proteins alone poorly stimulate ERK2, whereas a combination of both led to synergistic effects. We conclude that dually coupled GPCRs require a cooperation of Gαi- and Gq/11-mediated pathways for efficient stimulation of the ERK cascade. Cooperative signaling by multiple G proteins thus might represent a novel concept implicated in the regulation of cellular responses by GPCRs.

scholarly journals Essential Role for G Protein-coupled Receptor Endocytosis in the Activation of Mitogen-activated Protein Kinase

1998 ◽  
Vol 273 (2) ◽  
pp. 685-688 ◽  
Author(s):  
Yehia Daaka ◽  
Louis M. Luttrell ◽  
Seungkirl Ahn ◽  
Gregory J. Della Rocca ◽  
Stephen S. G. Ferguson ◽  
...  
Keyword(s):  
Protein Kinase ◽  
G Protein ◽  
Essential Role ◽  
Mitogen Activated Protein Kinase ◽  
G Protein Coupled Receptor ◽  
Receptor Endocytosis ◽  
Mitogen Activated Protein ◽  
G Protein Coupled

Aluminum potentiates P(i) transport stimulation induced by fluoride in osteoblast-like cells

1996 ◽  
Vol 271 (4) ◽  
pp. E694-E701
Author(s):  
T. Imai ◽  
D. Burgener ◽  
X. Zhen ◽  
J. P. Benjour ◽  
J. Caverzasio
Keyword(s):  
Protein Kinase ◽  
Tyrosine Phosphorylation ◽  
G Protein ◽  
Calf Serum ◽  
Mitogen Activated Protein Kinase ◽  
Dependent Manner ◽  
Deferoxamine Mesylate ◽  
Mitogen Activated Protein ◽  
Umr 106 ◽  
G Protein Coupled

The effect of aluminum (AI) on inorganic phosphate (P(i)) transport stimulation induced by fluoride (F) was investigated in MC3T3-E1 osteoblast-like cells. Al potentiated the increase in P(i) transport activity induced by F in a dose- and time-dependent manner. Results obtained with deferoxamine mesylate, an Al chelator, suggest that a fluoroalumino complex is probably the active F molecule responsible for the change in P(i) transport observed in this study. The signaling pathway responsible for the stimulation of P(i) transport by F+Al likely involves a tyrosine phosphorylation process but neither a protein kinase C nor a mitogen-activated protein kinase pathway. As previously found in UMR-106 cells for F alone, F+Al potentiated the change in P(i) transport induced by fetal calf serum. A similar interaction was found between F+Al and thrombin acting through a G protein-coupled receptor. These observations are compatible with the hypothesis that F+Al could interact with G protein-coupled receptors associated with a signaling tyrosine phosphorylation process involved in the regulation of P(i), transport in osteoblast-like cells.

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