Room 302, 10/17/2000 9: 00 AM - 10: 30 AM (PD) Phosphorylation of p90 Ribosomal S6 Kinase by Mitogen-Activated Protein Kinase in the Signal Transduction Pathway of the μ Opioid Receptor 

2000 ◽  
Vol 93 (3A) ◽  
pp. A-126
Author(s):  
Takehiro Shoda ◽  
Hisatoshi Uga ◽  
Hiroyuki Mima ◽  
Kazuhiko Fukuda
Keyword(s):  
Signal Transduction ◽  
Protein Kinase ◽  
Opioid Receptor ◽  
Signal Transduction Pathway ◽  
Mitogen Activated Protein Kinase ◽  
Transduction Pathway ◽  
S6 Kinase ◽  
Mitogen Activated Protein ◽  
Μ Opioid Receptor ◽  
Ribosomal S6 Kinase

Far1 and Fus3 link the mating pheromone signal transduction pathway to three G1-phase Cdc28 kinase complexes

1993 ◽  
Vol 13 (9) ◽  
pp. 5659-5669 ◽  
Author(s):  
M Tyers ◽  
B Futcher
Keyword(s):  
Signal Transduction ◽  
Protein Kinase ◽  
Signal Transduction Pathway ◽  
Mitogen Activated Protein Kinase ◽  
G1 Phase ◽  
Transduction Pathway ◽  
Yeast Saccharomyces Cerevisiae ◽  
Alpha Factor ◽  
Mitogen Activated Protein

In the yeast Saccharomyces cerevisiae, the Cdc28 protein kinase controls commitment to cell division at Start, but no biologically relevant G1-phase substrates have been identified. We have studied the kinase complexes formed between Cdc28 and each of the G1 cyclins Cln1, Cln2, and Cln3. Each complex has a specific array of coprecipitated in vitro substrates. We identify one of these as Far1, a protein required for pheromone-induced arrest at Start. Treatment with alpha-factor induces a preferential association and/or phosphorylation of Far1 by the Cln1, Cln2, and Cln3 kinase complexes. This induced interaction depends upon the Fus3 protein kinase, a mitogen-activated protein kinase homolog that functions near the bottom of the alpha-factor signal transduction pathway. Thus, we trace a path through which a mitogen-activated protein kinase regulates a Cdc2 kinase.

Clozapine and the mitogen-activated protein kinase signal transduction pathway: Implications for antipsychotic actions

2005 ◽  
Vol 57 (6) ◽  
pp. 617-623 ◽  
Author(s):  
Jeff L. Browning ◽  
Tushar Patel ◽  
Paul C. Brandt ◽  
Keith A. Young ◽  
Leigh A. Holcomb ◽  
...  
Keyword(s):  
Signal Transduction ◽  
Protein Kinase ◽  
Signal Transduction Pathway ◽  
Mitogen Activated Protein Kinase ◽  
Transduction Pathway ◽  
Mitogen Activated Protein

scholarly journals p42 mitogen-activated protein kinase and p90 ribosomal S6 kinase are selectively phosphorylated and activated during thrombin-induced platelet activation and aggregation.

1994 ◽  
Vol 14 (1) ◽  
pp. 463-472 ◽  
Author(s):  
J Papkoff ◽  
R H Chen ◽  
J Blenis ◽  
J Forsman
Keyword(s):  
Signal Transduction ◽  
Platelet Aggregation ◽  
Protein Kinase ◽  
Immune Complex ◽  
Platelet Activation ◽  
Kinase Activity ◽  
Mitogen Activated Protein Kinase ◽  
S6 Kinase ◽  
Mitogen Activated Protein ◽  
Ribosomal S6 Kinase

Human platelets provide an excellent model system for the study of phosphorylation events during signal transduction and cell adhesion. Platelets are terminally differentiated cells that exhibit rapid phosphorylation of many proteins upon agonist-induced activation and aggregation. We have sought to identify the kinases as well as the phosphorylated substrates that participate in thrombin-induced signal transduction and platelet aggregation. In this study, we have identified two forms of mitogen-activated protein kinase (MAPK), p42mapk and p44mapk, in platelets. The data demonstrate that p42mapk but not p44mapk becomes phosphorylated on serine, threonine, and tyrosine during platelet activation. Immune complex kinase assays, gel renaturation assays, and a direct assay for MAPK activity in platelet extracts all support the conclusion that p42mapk but not p44mapk shows increased kinase activity during platelet activation. The activation of p42mapk, independently of p44mapk, in platelets is unique since in other systems, both kinases are coactivated by a variety of stimuli. We also show that platelets express p90rsk, a ribosomal S6 kinase that has previously been characterized as a substrate for MAPK. p90rsk is phosphorylated on serine in resting platelets, and this phosphorylation is enhanced upon thrombin-induced platelet activation. Immune complex kinase assays demonstrate that the activity of p90rsk is markedly increased during platelet activation. Another ribosomal S6 protein kinase, p70S6K, is expressed by platelets but shows no change in kinase activity upon platelet activation with thrombin. Finally, we show that the increased phosphorylation and activity of both p42mapk and p90rsk does not require integrin-mediated platelet aggregation. Since platelets are nonproliferative cells, the signal transduction pathways that include p42mapk and p90rsk cannot lead to a mitogenic signal and instead may regulate cytoskeletal or secretory changes during platelet activation.

scholarly journals Association of the Ras to Mitogen-activated Protein Kinase Signal Transduction Pathway with Microfilaments

1999 ◽  
Vol 274 (36) ◽  
pp. 25659-25667 ◽  
Author(s):  
Coralie A. Carothers Carraway ◽  
Maria E. Carvajal ◽  
Kermit L. Carraway
Keyword(s):  
Signal Transduction ◽  
Protein Kinase ◽  
Signal Transduction Pathway ◽  
Mitogen Activated Protein Kinase ◽  
Transduction Pathway ◽  
Mitogen Activated Protein

p42 mitogen-activated protein kinase and p90 ribosomal S6 kinase are selectively phosphorylated and activated during thrombin-induced platelet activation and aggregation

1994 ◽  
Vol 14 (1) ◽  
pp. 463-472
Author(s):  
J Papkoff ◽  
R H Chen ◽  
J Blenis ◽  
J Forsman
Keyword(s):  
Signal Transduction ◽  
Platelet Aggregation ◽  
Protein Kinase ◽  
Immune Complex ◽  
Platelet Activation ◽  
Kinase Activity ◽  
Mitogen Activated Protein Kinase ◽  
S6 Kinase ◽  
Mitogen Activated Protein ◽  
Ribosomal S6 Kinase

Human platelets provide an excellent model system for the study of phosphorylation events during signal transduction and cell adhesion. Platelets are terminally differentiated cells that exhibit rapid phosphorylation of many proteins upon agonist-induced activation and aggregation. We have sought to identify the kinases as well as the phosphorylated substrates that participate in thrombin-induced signal transduction and platelet aggregation. In this study, we have identified two forms of mitogen-activated protein kinase (MAPK), p42mapk and p44mapk, in platelets. The data demonstrate that p42mapk but not p44mapk becomes phosphorylated on serine, threonine, and tyrosine during platelet activation. Immune complex kinase assays, gel renaturation assays, and a direct assay for MAPK activity in platelet extracts all support the conclusion that p42mapk but not p44mapk shows increased kinase activity during platelet activation. The activation of p42mapk, independently of p44mapk, in platelets is unique since in other systems, both kinases are coactivated by a variety of stimuli. We also show that platelets express p90rsk, a ribosomal S6 kinase that has previously been characterized as a substrate for MAPK. p90rsk is phosphorylated on serine in resting platelets, and this phosphorylation is enhanced upon thrombin-induced platelet activation. Immune complex kinase assays demonstrate that the activity of p90rsk is markedly increased during platelet activation. Another ribosomal S6 protein kinase, p70S6K, is expressed by platelets but shows no change in kinase activity upon platelet activation with thrombin. Finally, we show that the increased phosphorylation and activity of both p42mapk and p90rsk does not require integrin-mediated platelet aggregation. Since platelets are nonproliferative cells, the signal transduction pathways that include p42mapk and p90rsk cannot lead to a mitogenic signal and instead may regulate cytoskeletal or secretory changes during platelet activation.

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