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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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Nerve growth factor signaling, neuroprotection, and neural repair
TL;DR: Expanded roles for NGF that are associated with the dynamically regulated production of NGF and its receptors that begins in development, extends throughout adult life and aging, and involves a surprising variety of neurons, glia, and nonneural cells are considered.
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An essential role for Rho, Rac, and Cdc42 GTPases in cell cycle progression through G1
TL;DR: When microinjected into quiescent fibroblasts, Rho, Rac, and Cdc42 stimulated cell cycle progression through G1 and subsequent DNA synthesis, and microinjection of dominant negative forms of Rac and CDC42 or of the Rho inhibitor C3 transferase blocked serum-induced DNA synthesis.
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Multiple docking sites on substrate proteins form a modular system that mediates recognition by ERK MAP kinase
TL;DR: It is shown that the amino acid sequence FXFP is an evolutionarily conserved docking site that mediates ERK MAP kinase binding to substrates in multiple protein families, suggesting that the partially overlapping substrate specificities of ERK and JNK result from recognition of shared and unique docking sites.
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Matrix adhesion and Ras transformation both activate a phosphoinositide 3-OH kinase and protein kinase B/Akt cellular survival pathway
TL;DR: PI 3‐kinase acting through PKB/Akt is implicated as a key mediator of the aberrant survival of Ras‐transformed epithelial cells in the absence of attachment, and mediates matrix‐induced survival of normal epithelial Cells.
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Parallel signal processing among mammalian MAPKs
Eva Cano,Louis C. Mahadevan +1 more
TL;DR: The recent discovery of two other MAPK subtypes, the JNK/SAPK subfamily and p38/RK (mammalian equivalents of HOG1 in yeast), reveals extreme complexity within the family and the existence in mammalian cells of parallel MAPK cascades that can be activated simultaneously.
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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.