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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 deaf and the dumb: the biology of ErbB-2 and ErbB-3
TL;DR: This review highlights recent structural insights into the mechanism of ligand-induced heterodimer formation, and concentrates on signaling pathways employed by ErBB-2 and ErbB-3 in normal and in malignant cells.
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Role of reactive aldehyde in cardiovascular diseases.
TL;DR: The protein-bound aldehydes can be detected as constituents not only in in vitro oxidized low-density lipoproteins but also in animal models of atherosclerosis and in human patients with increased risk factors or clinical manifestations of Atherosclerosis, indicating that they could indeed be involved in the caldiovascular pathology.
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Activation of phosphoinositide 3-kinase by interaction with Ras and by point mutation.
Pablo Rodriguez-Viciana,Patricia H. Warne,Bart Vanhaesebroeck,Michael D. Waterfield,Julian Downward +4 more
TL;DR: The data show that PI 3‐kinase is regulated by a number of mechanisms, and that Ras contributes to the activation of this lipid kinase synergistically with tyrosine kinases.
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Functions of NF-κB1 and NF-κB2 in immune cell biology
Sören Beinke,Steven C. Ley +1 more
TL;DR: In this article, the authors focus on the latest advances in research on the function of NF-κB1/Rel transcription factor in immune cells and present a review of the most recent advances in this area.
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Stimulation of the Stress-Activated Mitogen-Activated Protein Kinase Subfamilies in Perfused Heart: p38/RK Mitogen-Activated Protein Kinases and c-Jun N-Terminal Kinases Are Activated by Ischemia/Reperfusion
Marie A. Bogoyevitch,Judith Gillespie-Brown,Albert J. Ketterman,Stephen J. Fuller,Rachel Ben-Levy,Alan Ashworth,Christopher John Marshall,Peter H. Sugden +7 more
TL;DR: Using the isolated perfused rat heart, it is shown that global ischemia does not activate the 42- and 44-kD extracellular signal-regulated (protein) kinase (ERK) subfamily of MAPKs but rather stimulates a 38- kD activator ofMAPK-activated protein kinase-2 (MAPKAPK2) which is maintained during reperfusion.
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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.