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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

Insulin Signaling in the Yeast Saccharomyces cerevisiae. 3. Induction of Protein Phosphorylation by Human Insulin

TL;DR: The data presented raise the possibility that stimulation of glycogen synthesis by insulin in yeast is mediated by a 53-kDa insulin-binding protein and a 70-k da phosphotyrosine-containing protein which are organized in a large plasma membrane-bound signaling complex.
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Targeted genomic disruption of H-ras and N-ras has no effect on early renal changes after unilateral ureteral ligation

TL;DR: The activation of H-ras and N-ras isoforms does not play a major role in the early renal damage induced by UUO, and morphological alterations in the O kidneys were similar to those revealed by histological and immunohistochemical studies.
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Silencing Aurora A leads to re-sensitization of breast cancer cells to Taxol through downregulation of SRC-mediated ERK and mTOR pathways

TL;DR: Results suggested that the activation of Aurora A and the subsequent upregulation of ERK and Akt through SRC induced Taxol-resistance in breast cancer cells, and inhibiting Aurora B and the related SRC/EKT/Akt pathway could restore the sensitivity of breast cancers cells to Taxol.
Journal ArticleDOI

Redox regulation of signal transduction in smooth muscle cells: distinct effects of PKC-down regulation and PKC inhibitors on oxidant induced MAP kinase.

TL;DR: The results suggest that oxidant-induced mitogen activated protein kinase isprotein kinase C independent, and are in line with previous results suggesting that reactive oxygen species function as signaling molecules, and reactive oxygen Species are generated under both normal and pathological conditions.
Journal ArticleDOI

Mechanism of CK2.3, a Novel Mimetic Peptide of Bone Morphogenetic Protein Receptor Type IA, Mediated Osteogenesis.

TL;DR: CK 2.3 is a novel peptide that drives osteogenesis, and the molecular sequence of events that are triggered from the stimulation of CK2.3 until the induction of mineralization can be applied in the development of future therapeutics for osteoporosis.
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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