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Journal ArticleDOI

MAP kinase kinase kinase, MAP kinase kinase and MAP kinase.

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.
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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.

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Journal ArticleDOI

ASK1 Inhibits Interleukin-1-induced NF-κB Activity through Disruption of TRAF6-TAK1 Interaction

TL;DR: It appears that the inhibition of NF-κB by ASK1 may result at least in part from the disruption of the TRAF6·TAK1 complex formation in the IL-1 signaling pathway.
Journal ArticleDOI

Identification and functional analysis of a developmentally regulated extracellular signal-regulated kinase gene in Dictyostelium discoideum.

TL;DR: The results indicate that ERK1 plays an essential role during the growth and differentiation of D. discoideum and Antisense mutagenesis from a derepressible promoter indicates that the gene is essential for vegetative growth.
Journal Article

Alpha2-adrenergic agonists selectively activate extracellular signal-regulated kinases in Müller cells in vivo.

TL;DR: The results indicate that systemically administered alpha2-adrenergic agonists selectively activate ERKs in retinal Müller cells, indicating one of the early events that result in photoreceptor protection.
Journal ArticleDOI

Caenorhabditis elegans lin-45 raf Is Essential for Larval Viability, Fertility and the Induction of Vulval Cell Fates

TL;DR: The analysis of the missense mutations indicates that Ras binding, 14-3- 3-binding, and protein kinase activity are necessary for full Raf function and suggests that a 14-2-3 protein positively regulates Raf-mediated signaling during C. elegans development.
Journal ArticleDOI

Activated G Protein-coupled Receptor Induces Tyrosine Phosphorylation of STAT3 and Agonist-selective Serine Phosphorylation via Sustained Stimulation of Mitogen-activated Protein Kinase RESULTANT EFFECTS ON CELL PROLIFERATION

TL;DR: The difference in the magnitude of the proliferative response evoked by the two agonists at the sst4 receptor can be accounted for by their differential ability to phosphorylate STAT3 on serine residues and supports the concept that selective signaling can be achieved through pharmacological diversity.
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.
Journal ArticleDOI

ERKs: A family of protein-serine/threonine kinases that are activated and tyrosine phosphorylated in response to insulin and NGF

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.
Journal ArticleDOI

Raf-1 activates MAP kinase-kinase.

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.
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