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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The GRB family of SH2 domain proteins
TL;DR: The cloning of SH2 domain proteins based on their binding to growth factor receptors is a powerful technique to elucidate new signaling pathways and its ability to identify novel signaling cascades that can emanate from tyrosine kinases is identified.
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p38α Isoform Mxi2 Binds to Extracellular Signal-Regulated Kinase 1 and 2 Mitogen-Activated Protein Kinase and Regulates Its Nuclear Activity by Sustaining Its Phosphorylation Levels
TL;DR: The findings point to Mxi2 as a unique member of the p38 family that may have an unprecedented role in the regulation of the functions of ERK mitogen-activated protein kinases.
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Antisense protein tyrosine phosphatase 1B reverses activation of p38 mitogen-activated protein kinase in liver of ob/ob mice.
Rebecca J. Gum,Lori L. Gaede,Matthew Heindel,Jeffrey F. Waring,James M. Trevillyan,Bradley A. Zinker,Margery E. Stark,Denise Wilcox,Michael R. Jirousek,Cristina M. Rondinone,Roger G. Ulrich +10 more
TL;DR: It is demonstrated that reduction of PTP1B protein using ASO reduces activation of p38 and its substrates TNFalpha and CREB in liver of diabetic mice, which correlates with decreased hyperglycemia and hyperinsulinemia.
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Two Naturally Occurring Mutant Insulin Receptors Phosphorylate Insulin Receptor Substrate-1 (IRS-1) but Fail to Mediate the Biological Effects of Insulin EVIDENCE THAT IRS-1 PHOSPHORYLATION IS NOT SUFFICIENT FOR NORMAL INSULIN ACTION
TL;DR: The inability of these mutant receptors to signal normally to metabolic and mitogenic responses suggests that insulin-stimulated tyrosine phosphorylation of IRS-1 alone is insufficient to fully mediate insulin action.
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Induction of Nrf2/ARE-mediated cytoprotective genes by red ginseng oil through ASK1–MKK4/7–JNK and p38 MAPK signaling pathways in HepG2 cells
Min Ji Bak,Min Ji Bak,Van-Long Truong,Se-Yeon Ko,Xuan Ngan Giang Nguyen,Mira Jun,Soon-Gi Hong,Jong-Won Lee,Woo-Sik Jeong +8 more
TL;DR: RGO could be used as a potential chemopreventive agent, possibly by induction of Nrf2/ARE-mediated phase II enzymes via ASK1–MKK4/7–JNK and p38 MAPK signaling pathways.
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.