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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Vitamin E analog modulates UVB-induced signaling pathway activation and enhances cell survival
TL;DR: UVB-induced signaling pathway activation is differentially modulated by Trolox, and modulation of signal transduction with cell outcome should facilitate development of rational strategies for pharmacologic applications.
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The Mitogen-Activated Protein Kinase CgMK1 Governs Appressorium Formation, Melanin Synthesis, and Plant Infection of Colletotrichum gloeosporioides.
TL;DR: It is concluded that CgMK1 plays a vital role in regulating appressorium formation, melanin biosynthesis, and virulence in C. gloeosporiodes.
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Myeloid leukemia cell growth and differentiation are independent of mitogen-activated protein kinase ERK1/2 activation.
TL;DR: The results indicate that ERK1/2 activation is not an essential requirement for leukemic cell growth and differentiation and that within the same cell line, differentiation to a given lineage could occur with and without ERK2 activation, depending on the stimulus.
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Programmed cell death in C. elegans.
TL;DR: In this review, the current models of cell death regulation and execution in C. elegans are set out, focussing in particular on the similarities between cell death in C .
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The Cell Surface Protein Gene ecm33+ Is a Target of the Two Transcription Factors Atf1 and Mbx1 and Negatively Regulates Pmk1 MAPK Cell Integrity Signaling in Fission Yeast
Hirofumi Takada,Aiko Nishida,Mitsuhiro Domae,Ayako Kita,Yuki Yamano,Atsushi Uchida,Shunji Ishiwata,Yue Fang,Xin Zhou,Takashi Masuko,Mitsuhiro Kinoshita,Kazuaki Kakehi,Reiko Sugiura +12 more
TL;DR: The identified and characterized ecm33+, which encodes a GPI-anchored cell surface protein as a transcriptional target of Atf1 and Mbx1, and demonstrates real-time monitoring of the activation of the cell integrity MAPK signaling pathway.
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.