Journal ArticleDOI
MAP kinase kinase kinase, MAP kinase kinase and MAP kinase.
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TLDR
Recent advances have shown that in two MAP kinase pathways (the mating response pathway in the fission yeast Schizosaccharomyces pombe, and receptor tyrosine kinase signalling), the small GTP binding protein ras p21 links membrane events to kinase pathway activation.About:
This article is published in Current Opinion in Genetics & Development.The article was published on 1994-02-01. It has received 987 citations till now. The article focuses on the topics: MAP kinase kinase kinase & Mitogen-activated protein kinase kinase.read more
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Ligation of the α2M Signalling Receptor Elevates the Levels of p21Ras-GTP in Macrophages
Uma K. Misra,Salvatore V. Pizzo +1 more
TL;DR: The mitogenic effects of ligating alpha2MSR are mediated through a Ras-dependent pathway, and the formation of p2 Ras-GTP in murine peritoneal macrophages upon treatment with alpha2M-methylamine and RBF is studied.
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Increased activity of MAP, p70S6 and p90rs kinases is associated with AP-1 activation in spontaneous liver tumours, but not in adjacent tissue in mice.
Jerzy Ostrowski,M. Woszczynski,P Kowalczyk,T Wocial,Ewa E. Hennig,L Trzeciak,P Janik,Karol Bomsztyk +7 more
TL;DR: Constitutively activated kinases and AP-1 transcription factor found in hepatic malignancies are reminiscent of cells activated by EGF, suggesting that EGF and its intracellular effectors play a role in these malignancy.
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Osmostress induces autophosphorylation of Hog1 via a C-terminal regulatory region that is conserved in p38α.
TL;DR: It is shown that the yeast MAPK Hog1, known to be activated by the MAP2K Pbs2, is activated in pbs2Δ cells via an autophosphorylation activity that is induced by osmotic pressure.
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Cellular response to bioactive lipid peroxidation products.
TL;DR: It is argued that lipid mediators could induce a cellular process that represents a cellular defense program against toxic compounds, in which aldehyde-stimulated detoxification response is mediated by cyclooxygenase metabolites.
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Requirement for Metalloproteinase‐dependent ERK and AKT Activation in UVB‐induced G1‐S Cell Cycle Progression of Human Keratinocytes
Weinong Han,Yu-Ying He +1 more
TL;DR: It is demonstrated that low doses of UVB induce keratinocyte proliferation and cell cycle progression of human HaCaT keratinocytes and metalloproteinase (MP) inhibitor GM6001 blocked UVB‐induced ERK and AKT activation,cell cycle progression, and decreased the EGFR phosphorylation, demonstrating that MPs mediate the EG FR/ERK/AKT/cyclin D1 pathways and cell Cycle progression induced by UVB radiation.
References
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Mammalian Ras interacts directly with the serine/threonine kinase Raf
TL;DR: Raf interacts with wild-type and activated Ras, but not with an effector domain mutant of Ras or with a dominant-interfering Ras mutant, and this interaction is dependent on GTP bound to Ras.
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ERKs: A family of protein-serine/threonine kinases that are activated and tyrosine phosphorylated in response to insulin and NGF
Teri G. Boulton,Steven H. Nye,David J. Robbins,Nancy Y. Ip,Elizabeth Radzlejewska,Sharon D. Morgenbesser,Ronald A. DePinho,Nikos Panayotatos,Melanie H. Cobb,George D. Yancopoulos +9 more
TL;DR: Cl cloning and characterization of two ERK1-related kinases, ERK2 and ERK3, are described and evidence suggesting that there are additional ERK family members is provided, which may serve as intermediates that depend on tyrosine phosphorylation to activate serine/threonineosphorylation cascades.
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cPLA2 is phosphorylated and activated by MAP kinase.
TL;DR: Treatment of cells with agents that stimulate the release of arachidonic acid causes increased serine phosphorylation and activation of cytosolic phospholipase A2 (cPLA2).
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Phosphorylation of c- jun mediated by MAP kinases
TL;DR: Evidence is presented that mitogen-activated protein-serine (MAP) kinases (pp54 and pp42/44) specifically phosphorylate these sites and that their phosphorylation positively regulates the transacting activity of c-jun.
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Raf-1 activates MAP kinase-kinase.
John M. Kyriakis,Harald App,Xian-feng Zhang,Papia Banerjee,David L. Brautigan,Ulf R. Rapp,Joseph Avruch +6 more
TL;DR: Results indicate that c-Raf-1 is an immediate upstream activator of MAPK-K in vivo, the first physiological substrate of the c-raf-l protooncogene product to be identified.