-
5
-
-
0027338999
-
cPLA2 is Phosphorylated and Activated by MAP Kinase
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mapk is shown to phosphorylate and activate cytosolic phospholipase A2, which indicates that agonist-induced arachidonic acid release involves the MAPK pathway.
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(1993)
Cell
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Lin1
Wartmann2
Lin3
Knopf4
Seth5
Davis6
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6
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0025832626
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Structure, Expression and Regulation of Protein Kinases Involved in the Phosphorylation of Ribosomal Protein S6
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(1991)
J Biol Chem
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Erikson1
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11
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0026608787
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Nuclear Localization and Regulation of erk- and rsk-Encoded Protein Kinases
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of special interest, See [12∗bb∗bb].
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(1992)
Mol Cell Biol
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, pp. 915-927
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Chen1
Sarnecki2
Blenis3
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13
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0027215820
-
A Divergence in the MAP Kinase Regulatory Network Defined by MEK Kinase and Raf
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of outstanding interest, A murine homologue of the S. cerevisiae STE11 ‘MAPKKK’ is cloned and shown to activate MAPKK. These studies, therefore, demonstrate that, in addition to raf-1 p74, there are other activators of MAPKK.
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(1993)
Science
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Lange-Carter1
Pleiman2
Gardner3
Blumer4
Johnson5
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0023991154
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A Gene which Encodes a Predicted Protein Kinase can Restore some Functions of the Ras Gene in Fission Yeast
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(1988)
EMBO J
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Nadin-Davis1
Nasim2
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15
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0025806672
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Byr2, a Schizosaccharomyces pombe Gene Encoding a Protein Kinase Capable of Partial Suppression of the Ras1 Mutant Phenotype
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(1991)
Mol Cell Biol
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Wang1
Xu2
Riggs3
Rogers4
Wigler5
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16
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0026661615
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Order of Action of Components in the Yeast Pheromone Response Pathway Revealed with a Dominant Allele of the STE11 Kinase and the Multiple Phosphorylation of the STE7 Kinase
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(1992)
Genes Dev
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Cairns1
Ramer2
Kornberg3
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0025225363
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STE11 is a Protein Kinase Required for Cell-Type-Specific Transcription and Signal Transduction in Yeast
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(1990)
Genes Dev
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, pp. 1862-1874
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Rhodes1
Connell2
Errede3
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18
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-
0026774153
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Constitutive Mutants of the Protein Kinase STE11 Activate the Yeast Pheromone Response Pathway in the Absence of the G Protein
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(1992)
Genes Dev
, vol.6
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Stevenson1
Rhodes2
Errede3
Sprague4
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19
-
-
0027476416
-
MAP Kinase-Related FUS3 from S. cerevisiae is Activated by STE7 In Vitro
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of outstanding interest, The S. cerevisiae STE7 kinase is shown to be a dual specificity kinase which phosphorylates the TEY motif in the FUS3 ‘MAPK’.
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(1993)
Nature
, vol.362
, pp. 261-264
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Gartner1
Zhaoqing2
Nasmyth3
Ammerer4
Errede5
-
22
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-
0027531645
-
An Osmosensing Signal Transduction Pathway in Yeast
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of outstanding interest, Identification of a MAPK pathway in S. cerevisiae for osmotic regulation. This paper highlights the fact that MAPK pathways are involved in more than growth control.
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(1993)
Science
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, pp. 1760-1763
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Brewster1
de Valoir2
Dwyer3
Winter4
Gustin5
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23
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0027265711
-
Complementation of byr1 in Fission Yeast by Mammalian MAP Kinase Kinase Requires Coexpression of Raf Kinase
-
of outstanding interest, Depletion of S. pombe MAPKK byr1 is not complemented by mammalian MAPKK unless raf is also expressed. This shows that mammalian MAPKK and byr1 can recognize the same substrates but that their upstream regulation differ. It also demonstrates that Raf directly activates mammalian MAPK.
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(1993)
Nature
, vol.364
, pp. 349-352
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Hughes1
Ashworth2
Marshall3
-
24
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-
0027184134
-
Novel Members of the Mitogen-Activated Protein Kinase Activator Family in Xenopus laevis
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of outstanding interest, The Xenopus MAPKK2 is shown to complement deletion of MKK1/2 in the S. cerevisiae cell shape pathways, but not deletion of Ste7 or PBS2 in the mating response or osmotic regulation pathways.
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(1993)
Mol Cell Biol
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Yashar1
Kelley2
Yee3
Errede4
Zon5
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26
-
-
0027383821
-
Schizosaccharomyces pombe spk1 is a Tyrosine-Phosphorylated Protein Functionally Related to Xenopus Mitogen Activated Protein Kinase
-
of outstanding interest, Xenopus MAPK is shown to complement deficiency of spk1 in S. pombe showing functional conservation of the ‘MAPKs’.
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(1993)
Mol Cell Biol
, vol.13
, pp. 6427-6434
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Gotoh1
Nishida2
Shimanaki3
Toda4
Imai5
Yamamoto6
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0025120244
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Requirements for Integration of Signals from Two Distinct Phosphorylation Pathways for Activation of MAP Kinase
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(1990)
Nature
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Anderson1
Maller2
Tonks3
Sturgill4
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28
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0026509971
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MAP Kinase Activator from Insulin-Stimulated Skeletal Muscle is a Protein Threonine/Tyrosine Kinase
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(1992)
EMBO J
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Nakielny1
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Wu3
Sturgill4
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33
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0027407059
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A Protein Kinase Similar to MAP Kinase Activator Acts Downstream of the Raf Kinase in Drosophila
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of outstanding interest, A genetic screen in Drosophila for suppressors of a partially inactivated version of Raf led to the isolation of Ssor1, which is highly homologous to mammalian MAPKKs. These experiments therefore define a MAPKK downstream of Raf and the identification of the mutations in the suppressor alleles might reveal activated alleles of MAPKK.
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(1993)
Cell
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, pp. 407-414
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Tsuda1
Inoue2
You3
Mizuno4
Hata5
Lim6
Adachi-Yamada7
Ryo8
Masamune9
Nishida10
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0027463637
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cDNA Cloning of MAP Kinase Kinase Reveals Kinase Cascade Pathways in Yeasts to Vertebrates
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(1993)
EMBO J
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, pp. 787-794
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Kosako1
Nishida2
Gotoh3
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37
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0027217533
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Cloning and Characterization of Two Distinct Human Extracellular Signal-Regulated Kinase Activator Kinases, MEK1 and MEK2
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J Biol Chem
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Zheng1
Guan2
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0027513768
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Phosphorylation of Xenopus Mitogen-Activated Protein (MAP) Kinase Kinase by MAP Kinase Kinase Kinase and MAP Kinase
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J Biol Chem
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Matsuda1
Gotoh2
Nishida3
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42
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0026541205
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Requirements for Phosphorylation of MAP Kinase During Meiosis in Xenopus Oocytes
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(1992)
Science
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, pp. 212-215
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Posada1
Cooper2
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43
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0025875819
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Dissection of the Protein Kinase Cascade by which Nerve Growth Factor Activates MAP Kinases
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(1991)
Nature
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, pp. 170-173
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Gómez1
Cohen2
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46
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0026641090
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Activation of Mitogen-Activated Protein Kinase Kinase by v-Raf in NIH 3T3 Cells and In Vitro
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⊎⊎] show that cells expressing oncogene Raf have activated MAPK, and in vitro Raf kinase was shown to reactivate and phosphorylate MAPKK inactivated by phosphatase treatment. These experiments therefore indicate that Raf is upstream of MAPKK in a kinase cascade and might be a MAPKKK.
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(1992)
Science
, vol.257
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Dent1
Haser2
Haystead3
Vincent4
Roberts5
Sturgill6
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47
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0027370827
-
Reconstitution of the Raf-1-MEK-ERK Signal Transduction Pathway In Vitro
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of special interest, Purification of epitope-tagged Raf from a baculovirus-based expression system is used to demonstrate that it is unlikely that there is an intermediate between raf-1 p74 and MAPKK.
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(1993)
Mol Cell Biol
, vol.13
, pp. 6615-6620
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MacDonald1
Crews2
Wu3
Driller4
Clark5
Erikson6
McCormick7
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48
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0027161398
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Complex Formation Between RAS and RAF and Other Protein Kinases
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⊎⊎] show that Raf directly interacts with ras p21 in the GTP-bound active state but not in the GDP-bound state. This interaction requires the amino-terminal region of c-Raf-1 and an intact effector domain of ras p21. This paper also demonstrates that S. pombe byr1 binds to ras p21-GTP and that there is a direct interaction between the catalytic carboxy-terminal domain of c-Raf-1 and MAPKK.
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(1993)
Proc Natl Acad Sci USA
, vol.90
, pp. 6213-6217
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Van Aelst1
Barr2
Marcus3
Polverino4
Wigler5
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49
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-
0027388945
-
A Protein Factor for ras p21-Dependent Activation of Mitogen-Activated Protein (MAP) Kinase Through MAP Kinase Kinase
-
of outstanding interest, edn 4, A cytosolic extract for Xenopus oocytes is described that activates MAPKK in a ras p21 GTP-dependent manner. Such a system can therefore be used to reconstitute the MAPK pathway.
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(1993)
Proc Natl Acad Sci USA
, vol.90
, pp. 975-979
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Itoh1
Kaibuchi2
Masuda3
Yamamoto4
Matsuuro5
Maeda6
Shimizu7
Takai8
-
50
-
-
0027237273
-
ras
-
of outstanding interest, Expression of the amino-terminal domain of c-Raf-1 in transient transfections is shown to block the activation of the MAPK pathway by EGF, phorbol esters, serum and oncogenic ras p21. Inhibition is overcome by coexpression of c-raf-1 arguing that signals from these ligands to the MAPK pathway is mediated by raf-1 p74.
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(1993)
J Biol Chem
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, pp. 20232-20236
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Schaap1
van der Wal2
Howe3
Marshall4
van Blitterswijk5
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52
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0027240231
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i-Coupled Acetylcholine Muscarinic m2 Receptor Activation of Mitogen-activated Protein (MAP) Kinase Kinase and MAP Kinase
-
⊎] show that at least two heterotrimeric G protein coupled responses in mammalian cells that activate MAPK employ ras p21 and raf-1 p74. These signalling pathways therefore have possible parallels to the mating response pathway in S. pombe by utilising both a heterotrimeric G protien and ras p21.
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J Biol Chem
, vol.268
, pp. 19196-19199
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Winitz1
Russeli2
Qian3
Gardner4
Dwyer5
Johnson6
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54
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0026596576
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Serum-, TPA-, and Ras-Induced Expression from Ap-1/Ets-Driven Promoters Requires Raf-1 Kinase
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(1992)
Genes Dev
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, pp. 545-556
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Bruder1
Heidecker2
Rapp3
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55
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0026523559
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Ras Mediates Nerve Growth Factor Receptor Modulation of Three Signal-Transducing Protein Kinases: MAP Kinase, Raf-1, and RSK
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(1992)
Cell
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Wood1
Sarnecki2
Roberts3
Blenis4
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56
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0027250250
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Mammalian Ras Interacts Directly with the Serine/Threonine Kinase Raf
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⊎⊎].
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(1993)
Cell
, vol.74
, pp. 205-214
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Vojtek1
Hollenberg2
Cooper3
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57
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0027200883
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Direct Interaction of Ras and the Amino-Terminal Region of Raf-1 In Vitro
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⊎⊎].
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(1993)
Nature
, vol.364
, pp. 352-355
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Warne1
Viciana2
Downward3
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60
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0027048684
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The Protein Kinase Homologue Ste20p is Required to Link the Yeast Pheromone Response G-Protein βγ Subunits to Downstream Signalling Components
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(1992)
EMBO J
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, pp. 4815-4824
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Leberer1
Dignard2
Harcus3
Thomas4
Whiteway5
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61
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0027530380
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A Dominant Truncation Allele Identifies a Gene, STE20, that Encodes a Putative Protein Kinase Necessary for Mating in Saccharomyces cerevisiae
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edn 4
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(1993)
Proc Natl Acad Sci USA
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Ramer1
Davis2
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62
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0026584373
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Dominant Mutations in a Gene Encoding a Putative Protein Kinase (BCK1) Bypass the Requirement for a Saccharomyces cerevisiae Protein Kinase C Homolog
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(1992)
Mol Cell Biol
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Lee1
Levin2
-
64
-
-
0027364980
-
Critical Tyrosine Residues Regulate the Enzymatic and Biological Activity of Raf-1 Kinase
-
of special interest, Tyr340 and Tyr341 are shown to be phosphorylated when raf-1 p74 is coexpressed with an oncogenic tyrosine kinase. Mutation of these tyrosines to negatively charged residues activates the kinase activity of Raf against MAPKK while mutation to phenylalanine blocks the ability of Raf to be activated. These results indicate that Tyr340 and Tyr341 are important to Raf kinase activity and show that tyrosine phosphorylation could regulate activity of Raf.
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(1993)
Mol Cell Biol
, vol.13
, pp. 7170-7179
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Fabian1
Daar2
Morrison3
-
65
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0027168907
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Identification of the Major Phosphorylation Sites of the Raf-1 Kinase
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of outstanding interest, Ser259 is identified as the major growth factor regulated serine phosphorylation event on raf-1 p74.
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(1993)
J Biol Chem
, vol.268
, pp. 17309-17316
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Morrison1
Heidecker2
Rapp3
Copeland4
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67
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0027326410
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Protein Kinase Cα Activates Raf-1 by Direct Phosphorylation
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⊎] demonstrate that protein kinase C can phosphorylate raf-1 p74 and activate its auto-kinase activity. This direct phosphorylation of raf-1 p74 by protein kinase C may regulate its activity.
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(1993)
Nature
, vol.364
, pp. 249-252
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Kolch1
Heidecker2
Kochs3
Hummel4
Vahidi5
Mischak6
Finkenzeller7
Marmé8
Rapp9
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68
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0027184473
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Requirements for Raf and MAP Kinase Function during the Meiotic Maturation of Xenopus Oocytes
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(1993)
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Fabian1
Morrison2
Daar3
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69
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Raf-1 Protein Kinase Is Important for Progesterone-Induced Xenopus Oocyte Maturation and Acts Downstream of Mos
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Mol Cell Biol
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Muslin1
MacNicol2
Williams3
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71
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0027527919
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Specific Association of Activated MAP Kinase Kinase Kinase (Raf) with the Plasma Membrane of Ras-Transformed Retinal Cells
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of outstanding interest, In Ras transformed cells raf-1 p74 is shown to be plasma membrane-localized rather than cytosolic, suggesting that ras p21-GTP may assemble raf-1 p74 at the plasma membrane. In addition, it is shown that phosphatase treatment does not inactivate the ability of Raf to phosphorylate MAPKK.
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(1993)
Oncogene
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Traverse1
Cohen2
Paterson3
Marshall4
Rapp5
Grand6
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72
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0027482547
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Raf-1 Protein Kinase Activates the NF-κB Transcription Factor by Dissociating the Cytoplasmic NF-κB-IκB Complex
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of outstanding interest, edn 4, IκB is identified as a substrate of Raf showing that Raf may phosphorylate not only MAPKK but also other substrates.
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(1993)
Proc Natl Acad Sci USA
, vol.90
, pp. 9247-9251
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Li1
Sedivy2
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73
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0027385030
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Conditional Transformation of Cells and Rapid Activation of the Mitogen-Activated Protein Kinase Cascade by an Estradiol-Dependent Human Raf-1 Protein Kinase
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of outstanding interest, Steroid inducible v-raf constructs are used to show that transformation of raf-1 cells is associated with MAPKK but not MAPK activation. This suggests that activation of MAPK may not only require the activation of upstream kinases but also inactivation of phosphatases.
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(1993)
Mol Cell Biol
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Samuels1
Weber2
Bishop3
McMahon4
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74
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0027501802
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cAMP Antagonizes p21ras Directed Activation of Extracellular Signal-Regulated Kinase 2 and Phosphorylation of mSos Nucleotide Exchange Factor
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(1993)
EMBO J
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Burgering1
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van Weeren3
Chardin4
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0027716596
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Inhibition of cAMP of Ras-Dependent Activation of Raf
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⊎].
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(1993)
Science
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Cook1
McCormick2
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76
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0027772672
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Inhibition of the EGF-Activated MAP Kinase Signalling Pathway by Adenosine 3′,5′-Monophosphate
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⊎] show that activation of the cyclic AMPdependent kinase, protein kinase A, blocks activation of the MAPK pathway, probably by direct phosphorylation of raf-1p74.
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(1993)
Science
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Wu1
Dent2
Jelinek3
Wolfman4
Weber5
Sturgill6
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77
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0027337519
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Complexes of Ras-GTP with Raf-1 and Mitogen-Activated Protein Kinase Kinase
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of outstanding interest, Immobilized ras p21 was found to associate with raf-1 p74 and MAPKK from rat brain cytosols. This interaction was dependent on an intact effector domain in ras p21 and required normal Ras to be in GTP-bound state. If inactive raf-1 p74 can be activated by addition to such complexes, then this system could provide a means to study Raf activation.
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(1993)
Science
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Moodie1
Willumsen2
Weber3
Wolfman4
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Extracellular Signals and Reversible Protein Phosphorylation: What to Mek of It All
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Crews1
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Activation of Extracellular Signal-Regulated Kinase, ERK2, by p21ras Oncoprotein
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Leevers1
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82
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The Human CL100 Gene Encodes a Tyr/Thr-Protein Phosphatase which Potently and Specifically Inactivates MAP Kinase and Suppresses its Activation by Oncogenic Ras in Xenopus Oocyte Extracts.
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mapk in vitro and to inactivate it in vivo. This work raises the issues of how many phosphatases work on MAPK and if there are specific phosphatases of MAPKK, Raf etc.
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(1993)
Oncogene
, vol.8
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Alessi1
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Keyse3
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83
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MKP-1 (3CH134), an Immediate Early Gene Product, Is a Dual Specificity Phosphatase That Dephosphorylates MAP Kinase In Vivo
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Oxidative Stress and Heat Shock Induce a Human Gene Encoding a Protein-Tyrosine Phosphatase
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Keyse1
Emslie2
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85
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cDNA Sequence of a Growth Factor-Inducible Immediate Early Gene and Characterization of Its Encoded Protein
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Charles1
Abler2
Lau3
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