Mae mediates MAP kinase phosphorylation of Ets transcription factors in Drosophila

Nature ◽  
2001 ◽  
Vol 411 (6835) ◽  
pp. 330-334 ◽  
Author(s):  
David A. Baker ◽  
Blandine Mille-Baker ◽  
S. Mark Wainwright ◽  
David Ish-Horowicz ◽  
Nicholas J. Dibb
Keyword(s):  
Transcription Factors ◽  
Map Kinase ◽  
Ets Transcription Factors ◽  
Kinase Phosphorylation

scholarly journals Reciprocal Control of Osteogenic and Adipogenic Differentiation by ERK/MAP Kinase Phosphorylation of Runx2 and PPARγ Transcription Factors

2015 ◽  
Vol 231 (3) ◽  
pp. 587-596 ◽  
Author(s):  
Chunxi Ge ◽  
William P. Cawthorn ◽  
Yan Li ◽  
Guisheng Zhao ◽  
Ormond A. MacDougald ◽  
...  
Keyword(s):  
Transcription Factors ◽  
Map Kinase ◽  
Adipogenic Differentiation ◽  
Kinase Phosphorylation

Molecular Mechanisms Mediating Synapse-Specific Gene Expression During Development of the Neuromuscular Junction

1998 ◽  
Vol 23 (4) ◽  
pp. 390-395 ◽  
Author(s):  
Daniel Goldman ◽  
Mohan K. Sapru
Keyword(s):  
Gene Expression ◽  
Transcription Factors ◽  
Neuromuscular Junction ◽  
Map Kinase ◽  
Molecular Mechanisms ◽  
Specific Gene ◽  
Subunit Gene ◽  
Nicotinic Acetylcholine ◽  
Adult Skeletal Muscle ◽  
Ets Transcription Factors

Adult skeletal muscle locally expresses nicotinic acetylcholine receptors (nAChRs) at the neuromuscular junction by selective induction of their subunit-encoding genes (αβεδ) in endplate-associated myonuclei. Neuregulin/ARIA is a nerve-derived factor that is thought to be largely responsible for this local gene induction, Neuregulin/ARIA activates a Ras/MAP kinase signalling cascade, which ultimately induces nAChR ε-subunit gene expression via a 15 bp sequence that harbors a core Ets transcription factor binding site (GGA). Interestingly, this same sequence also appears to participate in extrajunctional repression of the ε-subunit gene. Muscle Ets 2 overexpression induces nAChR ε-subunit gene promoter activity, whereas a dominant/negative Ets blocks neuregulin-dependent induction. These results suggest that Ets transcription factors play a role in mediating synapse-specific and neuregulin-mediated motor neuron control of nAChR gene expression. Key words: nicotinic acetylcholine receptor, Ras, MAP kinase. Ets transcription factors, neuregulin, protein tyrosine phosphatases

scholarly journals Prostaglandin E2 Affects Differently the Release of Inflammatory Mediators from Resident Macrophages by LPS and Muramyl Tripeptides

1999 ◽  
Vol 8 (6) ◽  
pp. 295-303 ◽  
Author(s):  
Peter Dieter ◽  
Ute Hempel ◽  
Sabine Kamionka ◽  
Angelika Kolada ◽  
Birgit Malessa ◽  
...  
Keyword(s):  
Nitric Oxide ◽  
Transcription Factors ◽  
Map Kinase ◽  
Kupffer Cells ◽  
Neutralizing Antibodies ◽  
Target Cells ◽  
Tnf Α ◽  
Extracellular Regulated Kinase ◽  
Oxide Synthase ◽  
Rapid Activation

LPS and MTP-PE (liposome-encapsulatedN-acetylmuramyl-L-alanyl-D-isoglutaminyl-L-alanine-2-:[1',2'-dipalmitoyl-sni-glycero-3-(hydroxy-phosphoryl-oxyl)] etylamide) induce in liver macrophages a synthesis and release of TNF-α, nitric oxide and prostanoids. Both agents induce an expression of mRNA's encoding TNF-α, inducible nitric oxide synthase (iNOS) and cyclooxygenase (COX)-2, and of corresponding proteins. LPS and MTP-PE induce a rapid activation of the extracellular regulated kinase (ERK) isoenzymes-1 and -2. Inhibition of map kinase isoenzymes leads to a decreased release of TNF-α, nitric oxide and prostaglandin (PG) E2after both agents. The transcription factors NF-κB and AP-1 are strongly activated by LPS within 30 minutes. MTP-PE induces a weak activation of both transcription factors only after 5 hours. Inhibition of NF-κB inhibits the LPS- but not the MTP-PE-induced release of TNF-α, nitric oxide and PGE2. PGE2release after LPS is higher than after MTP-PE. Exogenously added PGE2inhibits the activation of map kinase and TNF-α release by LPS, but not by MTP-PE. Release of nitric oxide after LPS and MTP-PE is enhanced after prior addition of PGE2. PGD2is without any effect. MTP-PE, but not LPS, induces a cytotoxicity of Kupffer cells against P815 tumor target cells. The MTP-PE-induced cytotoxicity is reduced by TNF-α neutralizing antibodies, indicating the involvement of TNF-α. Thus our results suggest that the different potencies of LPS and MTP-PE as immunomodulators probably result from different actions on Kupffer cells, resulting in differences in the amounts and kinetics of released TNF-α and PGE2, and that PGE2plays an important regulatory role in the action of LPS, but not in the actions of MTP-PE.

scholarly journals Altered MAP kinase phosphorylation and impaired motor coordination in PTPRR deficient mice

2006 ◽  
Vol 101 (3) ◽  
pp. 829-840 ◽  
Author(s):  
Renato G. S. Chirivi ◽  
Yvet E. Noordman ◽  
Catharina E. E. M. Van der Zee ◽  
Wiljan J. A. J. Hendriks
Keyword(s):  
Map Kinase ◽  
Motor Coordination ◽  
Kinase Phosphorylation ◽  
Deficient Mice

Platelet activation byStreptococcus sanguinisis accompanied by MAP kinase phosphorylation

Platelets ◽  
2012 ◽  
Vol 24 (1) ◽  
pp. 6-14 ◽  
Author(s):  
Ahmed Y. Abdulrehman ◽  
Elke C. G. Jackson ◽  
Archibald McNicol
Keyword(s):  
Map Kinase ◽  
Platelet Activation ◽  
Kinase Phosphorylation

Functional Role of p38 Mitogen Activated Protein Kinase in Platelet Activation induced by a Thromboxane A2 Analogue and by 8-iso-prostaglandin F2 α

2002 ◽  
Vol 87 (05) ◽  
pp. 888-898 ◽  
Author(s):  
Stefania Gaino ◽  
Valeria Zuliani ◽  
Rosa Tommasoli ◽  
Donatella Benati ◽  
Riccardo Ortolani ◽  
...  
Keyword(s):  
Map Kinase ◽  
Platelet Activation ◽  
Tyrosine Kinases ◽  
Actin Polymerization ◽  
Shape Change ◽  
Specific Inhibitor ◽  
P38 Map Kinase ◽  
Mitogen Activated Protein Kinase ◽  
Mitogen Activated Protein ◽  
Kinase Phosphorylation

SummaryWe investigated similarities in the signaling pathways elicited by the F2 isoprostane 8-iso-PGF2α and by low doses of U46619 to induce platelet activation. Both 0.01-0.1 µmol/L U46619 and 0.01-1 µmol/L 8-isoPGF2α triggered shape change and filopodia extension, as well as adhesion to immobilized fibrinogen of washed platelets. At these doses the two platelet agonists failed to trigger secretion and aggregation, which were however induced by higher doses of U46619 (0.1-1 µmol/L). SB203580 (1-10 µmol/L), a specific inhibitor of the p38 mitogen activated protein (MAP) kinase blunted platelet shape change and adhesion induced by 0.05-1 µmol/L 8-iso-PGF2α and by 0.01 µmol/L U46619. These platelet responses were also inhibited by 20 µmol/L cytochalasin D, an inhibitor of actin polymerization, and 50 µmol/L piceatannol, an inhibitor of the Syk tyrosine kinases. Both 8-iso-PGF2α and U46619-induced p38 MAP kinase phosphorylation in suspended platelets and this was inhibited by piceatannol, indicating that Syk activation occurs upstream p38 MAP kinase phosphorylation. These findings suggest that the signaling pathway triggered by both 8-iso-PGF2α and low concentrations of U46619 to induce platelet adhesion and shape change implicates Syk, the p38 MAP kinase, and actin polymerization.

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