Signaling pathways mediated by the mitogen-activated protein (MAP) kinase kinase/MAP kinase cascade

1994 ◽  
Vol 56 (5) ◽  
pp. 548-553 ◽  
Author(s):  
Satoshi Matsuda ◽  
Yukiko Gotoh ◽  
Eisuke Nishida
Keyword(s):  
Map Kinase ◽  
Signaling Pathways ◽  
Map Kinase Cascade ◽  
Protein Map ◽  
Mitogen Activated Protein ◽  
Kinase Cascade ◽  
Map Kinase Kinase

scholarly journals Conditional transformation of cells and rapid activation of the mitogen-activated protein kinase cascade by an estradiol-dependent human raf-1 protein kinase.

1993 ◽  
Vol 13 (10) ◽  
pp. 6241-6252 ◽  
Author(s):  
M L Samuels ◽  
M J Weber ◽  
J M Bishop ◽  
M McMahon
Keyword(s):  
Protein Kinase ◽  
Map Kinase ◽  
Map Kinases ◽  
Growth Media ◽  
Hormone Binding ◽  
Map Kinase Cascade ◽  
Mitogen Activated Protein ◽  
Kinase Cascade ◽  
Hormone Binding Domain ◽  
Map Kinase Kinase

We report a strategy for regulating the activity of a cytoplasmic signaling molecule, the protein kinase encoded by raf-1. Retroviruses encoding a gene fusion between an oncogenic form of human p74raf-1 and the hormone-binding domain of the human estrogen receptor (hrafER) were constructed. The fusion protein was nontransforming in the absence of estradiol but could be reversibly activated by the addition or removal of estradiol from the growth media. Activation of hrafER was accompanied in C7 3T3 cells by the rapid, protein synthesis-independent activation of both mitogen-activated protein (MAP) kinase kinase and p42/p44 MAP kinase and by phosphorylation of the resident p74raf-1 protein as demonstrated by decreased electrophoretic mobility. The phosphorylation of p74raf-1 had no effect on the kinase activity of the protein, indicating that mobility shift is an unreliable indicator of p74raf-1 enzymatic activity. Removal of estradiol from the growth media led to a rapid inactivation of the MAP kinase cascade. These results demonstrate that Raf-1 can activate the MAP kinase cascade in vivo, independent of other "upstream" signaling components. Parallel experiments performed with rat1a cells conditionally transformed by hrafER demonstrated activation of MAP kinase kinase in response to estradiol but no subsequent activation of p42/p44 MAP kinases or phosphorylation of p74raf-1. This result suggests that in rat1a cells, p42/p44 MAP kinase activation is not required for Raf-1-mediated oncogenic transformation. Estradiol-dependent activation of p42/p44 MAP kinases and phosphorylation of p74raf-1 was, however, observed in rat1a cells expressing hrafER when the cells were pretreated with okadaic acid. This result suggests that the level of protein phosphatase activity may play a crucial role in the regulation of the MAP kinase cascade. Our results provide the first example of a cytosolic signal transducer being harnessed by fusion to the hormone-binding domain of the estrogen receptor. This conditional system not only will aid the elucidation of the function of Raf-1 but also may be more broadly useful for the construction of conditional forms of other kinases and signaling molecules.

Conditional transformation of cells and rapid activation of the mitogen-activated protein kinase cascade by an estradiol-dependent human raf-1 protein kinase

1993 ◽  
Vol 13 (10) ◽  
pp. 6241-6252
Author(s):  
M L Samuels ◽  
M J Weber ◽  
J M Bishop ◽  
M McMahon
Keyword(s):  
Protein Kinase ◽  
Map Kinase ◽  
Map Kinases ◽  
Growth Media ◽  
Hormone Binding ◽  
Map Kinase Cascade ◽  
Mitogen Activated Protein ◽  
Kinase Cascade ◽  
Hormone Binding Domain ◽  
Map Kinase Kinase

We report a strategy for regulating the activity of a cytoplasmic signaling molecule, the protein kinase encoded by raf-1. Retroviruses encoding a gene fusion between an oncogenic form of human p74raf-1 and the hormone-binding domain of the human estrogen receptor (hrafER) were constructed. The fusion protein was nontransforming in the absence of estradiol but could be reversibly activated by the addition or removal of estradiol from the growth media. Activation of hrafER was accompanied in C7 3T3 cells by the rapid, protein synthesis-independent activation of both mitogen-activated protein (MAP) kinase kinase and p42/p44 MAP kinase and by phosphorylation of the resident p74raf-1 protein as demonstrated by decreased electrophoretic mobility. The phosphorylation of p74raf-1 had no effect on the kinase activity of the protein, indicating that mobility shift is an unreliable indicator of p74raf-1 enzymatic activity. Removal of estradiol from the growth media led to a rapid inactivation of the MAP kinase cascade. These results demonstrate that Raf-1 can activate the MAP kinase cascade in vivo, independent of other "upstream" signaling components. Parallel experiments performed with rat1a cells conditionally transformed by hrafER demonstrated activation of MAP kinase kinase in response to estradiol but no subsequent activation of p42/p44 MAP kinases or phosphorylation of p74raf-1. This result suggests that in rat1a cells, p42/p44 MAP kinase activation is not required for Raf-1-mediated oncogenic transformation. Estradiol-dependent activation of p42/p44 MAP kinases and phosphorylation of p74raf-1 was, however, observed in rat1a cells expressing hrafER when the cells were pretreated with okadaic acid. This result suggests that the level of protein phosphatase activity may play a crucial role in the regulation of the MAP kinase cascade. Our results provide the first example of a cytosolic signal transducer being harnessed by fusion to the hormone-binding domain of the estrogen receptor. This conditional system not only will aid the elucidation of the function of Raf-1 but also may be more broadly useful for the construction of conditional forms of other kinases and signaling molecules.

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 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 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
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