scholarly journals Regulation of cotton (Gossypium hirsutum ) drought responses by mitogen-activated protein (MAP) kinase cascade-mediated phosphorylation of GhWRKY59

2017 ◽  
Vol 215 (4) ◽  
pp. 1462-1475 ◽  
Author(s):  
Fangjun Li ◽  
Maoying Li ◽  
Ping Wang ◽  
Kevin L. Cox ◽  
Liusheng Duan ◽  
...  
Keyword(s):  
Gossypium Hirsutum ◽  
Map Kinase ◽  
Map Kinase Cascade ◽  
Protein Map ◽  
Mitogen Activated Protein ◽  
Kinase Cascade

scholarly journals A Novel Regulatory Mechanism in the Mitogen-activated Protein (MAP) Kinase Cascade

1997 ◽  
Vol 272 (51) ◽  
pp. 32642-32648 ◽  
Author(s):  
Makoto Fukuda ◽  
Isamu Gotoh ◽  
Makoto Adachi ◽  
Yukiko Gotoh ◽  
Eisuke Nishida
Keyword(s):  
Map Kinase ◽  
Regulatory Mechanism ◽  
Map Kinase Cascade ◽  
Protein Map ◽  
Mitogen Activated Protein ◽  
Kinase Cascade

scholarly journals The Stress-activated Mitogen-activated Protein Kinase Signaling Cascade Promotes Exit from Mitosis

2006 ◽  
Vol 17 (7) ◽  
pp. 3136-3146 ◽  
Author(s):  
Vladimír Reiser ◽  
Katharine E. D’Aquino ◽  
Ly-Sha Ee ◽  
Angelika Amon
Keyword(s):  
Map Kinase ◽  
Mitogen Activated Protein Kinase ◽  
Hog Pathway ◽  
Hypertonic Stress ◽  
Map Kinase Cascade ◽  
Protein Map ◽  
Mitogen Activated Protein ◽  
Early Anaphase ◽  
Kinase Cascade ◽  
Protein Kinase Signaling

In budding yeast, a signaling network known as the mitotic exit network (MEN) triggers exit from mitosis. We find that hypertonic stress allows MEN mutants to exit from mitosis in a manner dependent on the high osmolarity glycerol (HOG) mitogen-activated protein (MAP) kinase cascade. The HOG pathway drives exit from mitosis in MEN mutants by promoting the activation of the MEN effector, the protein phosphatase Cdc14. Activation of Cdc14 depends on the Cdc14 early anaphase release network, a group of proteins that functions in parallel to the MEN to promote Cdc14 function. Notably, exit from mitosis is promoted by the signaling branch defined by the Sho1 osmosensing system, but not by the Sln1 osmosensor of the HOG pathway. Our results suggest that the stress MAP kinase pathway mobilizes programs to promote completion of the cell cycle and entry into G1 under unfavorable conditions.

scholarly journals Role of a Mitogen-Activated Protein Kinase Cascade in Ion Flux-Mediated Turgor Regulation in Fungi

2006 ◽  
Vol 5 (3) ◽  
pp. 480-487 ◽  
Author(s):  
Roger R. Lew ◽  
Natalia N. Levina ◽  
Lana Shabala ◽  
Marinela I. Anderca ◽  
Sergey N. Shabala
Keyword(s):  
Map Kinase ◽  
Mitogen Activated Protein Kinase ◽  
Wild Type ◽  
Turgor Regulation ◽  
Map Kinase Cascade ◽  
Protein Map ◽  
Mitogen Activated Protein ◽  
Kinase Cascade ◽  
Protein Kinase Cascade

ABSTRACT Fungi normally maintain a high internal hydrostatic pressure (turgor) of about 500 kPa. In response to hyperosmotic shock, there are immediate electrical changes: a transient depolarization (1 to 2 min) followed by a sustained hyperpolarization (5 to 10 min) prior to turgor recovery (10 to 60 min). Using ion-selective vibrating probes, we established that the transient depolarization is due to Ca2+ influx and the sustained hyperpolarization is due to H+ efflux by activation of the plasma membrane H+-ATPase. Protein synthesis is not required for H+-ATPase activation. Net K+ and Cl− uptake occurs at the same time as turgor recovery. The magnitude of the ion uptake is more than sufficient to account for the osmotic gradients required for turgor to return to its original level. Two osmotic mutants, os-1 and os-2, homologs of a two-component histidine kinase sensor and the yeast high osmotic glycerol mitogen-activated protein (MAP) kinase, respectively, have lower turgor than the wild type and do not exhibit the sustained hyperpolarization after hyperosmotic treatment. The os-1 mutant does not exhibit all of the wild-type turgor-adaptive ion fluxes (Cl− uptake increases, but net K+ flux barely changes and net H+ efflux declines) (os-2 was not examined). Both os mutants are able to regulate turgor but at a lower level than the wild type. Our results demonstrate that a MAP kinase cascade regulates ion transport, activation of the H+-ATPase, and net K+ and Cl− uptake during turgor regulation. Other pathways regulating turgor must also exist.

Genetic Analysis of rolled, Which Encodes a Drosophila Mitogen-Activated Protein Kinase

Genetics ◽  
1999 ◽  
Vol 153 (2) ◽  
pp. 763-771 ◽  
Author(s):  
Young-Mi Lim ◽  
Kimiko Nishizawa ◽  
Yoshimi Nishi ◽  
Leo Tsuda ◽  
Yoshihiro H Inoue ◽  
...  
Keyword(s):  
Map Kinase ◽  
Mitogen Activated Protein Kinase ◽  
Female Sterility ◽  
Tor Signaling ◽  
Map Kinase Cascade ◽  
Dominant Female ◽  
Protein Map ◽  
Mitogen Activated Protein ◽  
Kinase Cascade

Abstract Genetic and molecular characterization of the dominant suppressors of D-rafC110 on the second chromosome identified two gain-of-function alleles of rolled (rl), which encodes a mitogen-activated protein (MAP) kinase in Drosophila. One of the alleles, rlSu23, was found to bear the same molecular lesion as rlSem, which has been reported to be dominant female sterile. However, rlSu23 and the current stock of rlSem showed only a weak dominant female sterility. Detailed analyses of the rl mutations demonstrated moderate dominant activities of these alleles in the Torso (Tor) signaling pathway, which explains the weak dominant female sterility observed in this study. The dominant rl mutations failed to suppress the terminal class maternal-effect mutations, suggesting that activation of Rl is essential, but not sufficient, for Tor signaling. Involvement of rl in cell proliferation was also demonstrated by clonal analysis. Branching and integration of signals in the MAP kinase cascade is discussed.

Activation of MAP kinase and translocation with HSP27 in bombesin-induced contraction of rectosigmoid smooth muscle

1995 ◽  
Vol 269 (5) ◽  
pp. G683-G691 ◽  
Author(s):  
H. Yamada ◽  
J. Strahler ◽  
M. J. Welsh ◽  
K. N. Bitar
Keyword(s):  
Smooth Muscle ◽  
Map Kinase ◽  
Resting Cells ◽  
Kinase Activation ◽  
Sustained Contraction ◽  
Contraction Map ◽  
Map Kinase Cascade ◽  
Protein Map ◽  
Mitogen Activated Protein ◽  
Kinase Cascade

We have investigated whether mitogen-activated protein (MAP) kinase cascade is essential for sustained contraction of smooth muscle cells of the rabbit rectosigmoid. We have identified MAP kinase as one of the enzymes activated by bombesin, performed immunologic studies blocking the activation of MAP kinase, and conducted confocal localization of MAP kinase in relation to heat-shock protein (HSP27), postulated to be involved in the sustained contraction of smooth muscle. Immunoblotting revealed two forms of MAP kinase (42 and 44 kDa). Activation of MAP kinase by bombesin was rapid, reaching a maximum in 30 s and subsequently declining. [D-Phe6,Leu13,psi(CH2NH),Phe14]BN-(6-14), a potent bombesin antagonist, and protein kinase C (PKC) inhibitors 1-(5-isoquinolinylsulfonyl)-2-methylpiperazine, calphostin C, and chelerythrine inhibited the increase in MAP kinase induced by bombesin. Immunofluorescent dual labeling and confocal microscopy indicate that these two proteins are closely distributed in resting cells and that during bombesin-induced contraction MAP kinase translocates accompanied by HSP27. In conclusion, a series of events involving PKC activation, MAP kinase activation, and MAP kinase-HSP27 translocation could be the signaling pathway involved in bombesin-induced sustained contraction.

scholarly journals Precisely Ordered Phosphorylation Reactions in the p38 Mitogen-activated Protein (MAP) Kinase Cascade

2013 ◽  
Vol 288 (32) ◽  
pp. 23322-23330 ◽  
Author(s):  
John M. Humphreys ◽  
Alexander T. Piala ◽  
Radha Akella ◽  
Haixia He ◽  
Elizabeth J. Goldsmith
Keyword(s):  
Map Kinase ◽  
Map Kinase Cascade ◽  
Protein Map ◽  
Mitogen Activated Protein ◽  
Kinase Cascade

scholarly journals Inhibition of the mitogen activated protein (MAP) kinase cascade potentiates cell killing by low dose ionizing radiation in A431 human squamous carcinoma cells

Oncogene ◽  
1998 ◽  
Vol 16 (21) ◽  
pp. 2787-2796 ◽  
Author(s):  
Steven Carter ◽  
Kelly L Auer ◽  
Dean B Reardon ◽  
Michael Birrer ◽  
Paul B Fisher ◽  
...  
Keyword(s):  
Ionizing Radiation ◽  
Map Kinase ◽  
Low Dose ◽  
Squamous Carcinoma ◽  
Carcinoma Cells ◽  
Squamous Carcinoma Cells ◽  
Map Kinase Cascade ◽  
Protein Map ◽  
Mitogen Activated Protein ◽  
Kinase Cascade

scholarly journals Combined computational and experimental analysis reveals mitogen-activated protein kinase–mediated feedback phosphorylation as a mechanism for signaling specificity

2012 ◽  
Vol 23 (19) ◽  
pp. 3899-3910 ◽  
Author(s):  
Nan Hao ◽  
Necmettin Yildirim ◽  
Michal J. Nagiec ◽  
Stephen C. Parnell ◽  
Beverly Errede ◽  
...  
Keyword(s):  
Map Kinase ◽  
Mitogen Activated Protein Kinase ◽  
Invasive Growth ◽  
Kinase Activation ◽  
Signaling Specificity ◽  
Map Kinase Cascade ◽  
Protein Map ◽  
Mitogen Activated Protein ◽  
Kinase Cascade ◽  
Physiological Outcomes

Different environmental stimuli often use the same set of signaling proteins to achieve very different physiological outcomes. The mating and invasive growth pathways in yeast each employ a mitogen-activated protein (MAP) kinase cascade that includes Ste20, Ste11, and Ste7. Whereas proper mating requires Ste7 activation of the MAP kinase Fus3, invasive growth requires activation of the alternate MAP kinase Kss1. To determine how MAP kinase specificity is achieved, we used a series of mathematical models to quantitatively characterize pheromone-stimulated kinase activation. In accordance with the computational analysis, MAP kinase feedback phosphorylation of Ste7 results in diminished activation of Kss1, but not Fus3. These findings reveal how feedback phosphorylation of a common pathway component can limit the activity of a competing MAP kinase through feedback phosphorylation of a common activator, and thereby promote signal fidelity.

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