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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Ras CAAX peptidomimetic FTI-277 selectively blocks oncogenic Ras signaling by inducing cytoplasmic accumulation of inactive Ras-Raf complexes.
Edwina C. Lerner,Yimin Qian,Michelle A. Blaskovich,Renae D. Fossum,Andreas Vogt,Jiazhi Sun,Adrienne D. Cox,Channing J. Der,Andrew D. Hamilton,Saïd M. Sebti +9 more
TL;DR: The results demonstrate that FTI-277 blocks Ras oncogenic signaling by accumulating inactive Ras/Raf complexes in the cytoplasm, hence preventing constitutive activation of the MAPK cascade.
Journal ArticleDOI
The atf1 transcription factor is a target for the sty1 stress-activated map kinase pathway in fission yeast
Marc G. Wilkinson,M. Samuels,T. Takeda,W. M. Toone,Jia-Ching Shieh,Takashi Toda,Jonathan B. A. Millar,Nic Jones +7 more
TL;DR: It is shown that Atf1 associates stably and is phosphorylated by the Sty1 kinase in vitro, indicating that the interaction between AM and Sty1 is direct, highlighting a remarkable level of conservation in transcriptional control by stress-activated MAP kinase pathways between fission yeast and mammalian cells.
Journal ArticleDOI
Pyp1 and Pyp2 PTPases dephosphorylate an osmosensing MAP kinase controlling cell size at division in fission yeast.
TL;DR: It is concluded that Pyp1 and Pyp2 are tyrosine-specific MAP kinase phosphatases that inactivate an osmoregulatedMAP kinase, Sty1, which acts downstream of the Wis1 MAP kinases kinase to control cell size at division in fission yeast.
Journal ArticleDOI
Mechanistic Studies of the Dual Phosphorylation of Mitogen-activated Protein Kinase
James E. Ferrell,Ramesh R. Bhatt +1 more
TL;DR: The findings indicate that MAPKK-1* phosphorylates p42 MAPK by a two- Collision, distributive mechanism rather than a single-collision, processive mechanism, and provide a mechanistic basis for understanding how MAP kinase can convert graded inputs into switch-like outputs.
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The ETS domain protein Pointed-P2 is a target of MAP kinase in the Sevenless signal transduction pathway
TL;DR: Genetic and biochemical data are presented suggesting that MAP kinase controls neural development through phosphorylation of two antagonizing transcription factors of the ETS family, Van and PntP2.
References
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Journal ArticleDOI
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).
Journal ArticleDOI
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.
Journal ArticleDOI
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.