scholarly journals Specificity of Phosphorylation Responses to Mitogen Activated Protein (MAP) Kinase Pathway Inhibitors in Melanoma Cells

2017 ◽  
Vol 17 (4) ◽  
pp. 550-564 ◽  
Author(s):  
Joel Basken ◽  
Scott A. Stuart ◽  
Andrew J. Kavran ◽  
Thomas Lee ◽  
Christopher C. Ebmeier ◽  
...  
Keyword(s):  
Map Kinase ◽  
Melanoma Cells ◽  
Protein Map ◽  
Mitogen Activated Protein ◽  
Map Kinase Pathway ◽  
Kinase Pathway

scholarly journals The Colletotrichum lagenarium Ste12-Like Gene CST1 Is Essential for Appressorium Penetration

2003 ◽  
Vol 16 (4) ◽  
pp. 315-325 ◽  
Author(s):  
Gento Tsuji ◽  
Satoshi Fujii ◽  
Seiji Tsuge ◽  
Tomonori Shiraishi ◽  
Yasuyuki Kubo
Keyword(s):  
Map Kinase ◽  
Lipid Droplets ◽  
Map Kinases ◽  
Cellulose Membrane ◽  
Appressorium Formation ◽  
Colletotrichum Lagenarium ◽  
Protein Map ◽  
Mitogen Activated Protein ◽  
Map Kinase Pathway ◽  
Kinase Pathway

Colletotrichum lagenarium is the causal agent of anthracnose of cucumber. This fungus produces a darkly melanized infection structure, appressoria, to penetrate the host leaves. The C. lagenarium CMK1 gene, a homologue of the Saccharomyces cerevisiae FUS3/KSS1 mitogen-activated protein (MAP) kinase genes, was shown to regulate conidial germination, appressorium formation, and invasive growth. In S. cerevisiae, Ste12p is known to be a transcriptional factor downstream of Fus3p/Kss1p MAP kinases. To evaluate the CMK1 MAP kinase pathway, we isolated the Ste12 homologue CST1 gene from C. lagenarium and characterized. The cst1Δ strains were nonpathogenic on intact host leaves, but could form lesions when inoculated on wounded leaves. Conidia of the cst1Δ strains could germinate and form melanized appressoria on both host leaf surface and artificial cellulose membrane, but could not produce infectious hyphae from appressoria, suggesting that CST1 is essential for appressorium penetration in C. lagenarium. In addition, matured appressoria of the cst1Δ strains contained an extremely low level of lipid droplets compared with that of the wild-type strain. Lipid droplets were abundant in conidia of the cst1Δ strains, but rapidly disappeared during appressorium formation. This misscheduled lipid degradation might be related to the failure of appressorium penetration in the cst1Δ strain.

scholarly journals Activation of Mitogen-activated Protein (MAP) Kinase Pathway by Pervanadate, a Potent Inhibitor of Tyrosine Phosphatases

1996 ◽  
Vol 271 (36) ◽  
pp. 22251-22255 ◽  
Author(s):  
Zhizhuang Zhao ◽  
Zhongjia Tan ◽  
Curtis D. Diltz ◽  
Min You ◽  
Edmond H. Fischer
Keyword(s):  
Map Kinase ◽  
Potent Inhibitor ◽  
Tyrosine Phosphatases ◽  
Protein Map ◽  
Mitogen Activated Protein ◽  
Map Kinase Pathway ◽  
Kinase Pathway

scholarly journals A Mitogen-Activated Protein Kinase That Senses Nitrogen Regulates Conidial Germination and Growth in Aspergillus fumigatus

2004 ◽  
Vol 3 (2) ◽  
pp. 557-560 ◽  
Author(s):  
Tao Xue ◽  
C. Kim Nguyen ◽  
Angela Romans ◽  
Gregory S. May
Keyword(s):  
Protein Kinase ◽  
Aspergillus Fumigatus ◽  
Map Kinase ◽  
Conidial Germination ◽  
Mitogen Activated Protein Kinase ◽  
Protein Map ◽  
Mitogen Activated Protein ◽  
Map Kinase Pathway ◽  
Germination And Growth ◽  
Kinase Pathway

ABSTRACT We show that the mitogen-activated protein (MAP) kinase pathway that responds to osmotic stress in Aspergillus fumigatus is also involved in nutritional sensing. This MAP kinase regulates conidial germination in response to the nitrogen source and is activated upon starvation for either carbon or nitrogen during vegetative growth.

scholarly journals Mitogen-activated protein kinase activation is insufficient for growth factor receptor-mediated PC12 cell differentiation.

1995 ◽  
Vol 15 (7) ◽  
pp. 3644-3653 ◽  
Author(s):  
R R Vaillancourt ◽  
L E Heasley ◽  
J Zamarripa ◽  
B Storey ◽  
M Valius ◽  
...  
Keyword(s):  
Cell Differentiation ◽  
Growth Factor ◽  
Map Kinase ◽  
Pc12 Cells ◽  
Pc12 Cell ◽  
Growth Factor Receptor ◽  
Receptor Activation ◽  
Mitogen Activated Protein ◽  
Map Kinase Pathway ◽  
Kinase Pathway

When expressed in PC12 cells, the platelet-derived growth factor beta receptor (beta PDGF-R) mediates cell differentiation. Mutational analysis of the beta PDGF-R indicated that persistent receptor stimulation of the Ras/Raf/mitogen-activated protein (MAP) kinase pathway alone was insufficient to sustain PC12 cell differentiation. PDGF receptor activation of signal pathways involving p60c-src or the persistent regulation of phospholipase C gamma was required for PC12 cell differentiation. beta PDGF-R regulation of phosphatidylinositol 3-kinase, the GTPase-activating protein of Ras, and the tyrosine phosphatase, Syp, was not required for PC12 cell differentiation. In contrast to overexpression of oncoproteins involved in regulating the MAP kinase pathway, growth factor receptor-mediated differentiation of PC12 cells requires the integration of other signals with the Ras/Raf/MAP kinase pathway.

Dibucaine and Tetracaine Inhibit the Activation of Mitogen-activated Protein Kinase Mediated by L-type Calcium Channels in PC12 Cells 

1999 ◽  
Vol 91 (6) ◽  
pp. 1798-1798 ◽  
Author(s):  
Masumi Kansha ◽  
Taro Nagata ◽  
Kazuo Irita ◽  
Shosuke Takahashi
Keyword(s):  
Map Kinase ◽  
Pc12 Cells ◽  
Local Anesthetics ◽  
Mitogen Activated Protein ◽  
Ic50 Values ◽  
Map Kinase Pathway ◽  
Kinase Signaling Pathway ◽  
Kinase Pathway ◽  
Map Kinase Signaling Pathway ◽  
Ca2 Channels

Background An elevation of the intracellular calcium level, which is mediated by N-methyl-D-aspartate receptors and L-type Ca2+ channels both, activates the mitogen-activated protein (MAP) kinase signaling pathway involved in synaptic modification. It has recently been suggested that MAP kinase plays a role in coupling the synaptic excitation to gene expression in the nucleus of postsynaptic neurons. Because the effects of local anesthetics on cellular signal transduction in neuronal cells are not well-known, the authors investigated whether they affect the MAP kinase signaling pathway using PC12 cells. Methods The cells were stimulated with either 50 mM KCl or 1 microM ionomycin, and activated MAP kinase was thus immunoprecipitated. The immunocomplexes were then subjected to an Elk1 phosphorylation assay. Both the phosphorylation of MAP kinase and the induction of c-Fos were detected by immunoblotting. Results Pretreatment of the cells with 1 mM (ethylenedioxy)-diethyl-enedinitrilotetraacetic acid or 5 micron nifedipine blocked the MAP kinase activation induced by 50 mM KCl, whereas pretreatment with 2 microM omega-conotoxin GIVA did not. The expression of c-Fos induced by potassium chloride was also suppressed by dibucaine, tetracaine (concentrations that inhibited 50% of the activity of positive control [IC50s] were 16.2+/-0.2 and 73.2+/-0.7 microM, respectively), and PD 98059, a mitogen-activated/extracellular receptor-regulated kinase inhibitor. Higher concentrations of dibucaine and tetracaine were needed to suppress the activation of MAP kinase induced by ionomycin (the IC50 values of dibucaine and tetracaine were 62.5+/-2.2 and 330.5+/-32.8 microM, respectively) compared with potassium chloride (the IC50 values of dibucaine and tetracaine were 17.7+/-1.0 and 70.2+/-1.2 microM, respectively). Although probable targets of these local anesthetics might be L-type Ca2+ channels or components between Ca2+ and Ras in MAP kinase pathway, the possibility that they directly affect MAP kinase still remains. Conclusions Dibucaine and tetracaine at clinical concentrations were found to inhibit the activation of MAP kinase and the expression of c-Fos mediated by L-type Ca2+ channels in PC12 cells. The suppression of MAP kinase pathway may thus be a potential target site for the actions of dibucaine and tetracaine, including the modification of the synaptic functions.

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