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.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
Citations
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Journal ArticleDOI
Differential genetic interactions of yeast stress response MAPK pathways.
Humberto Martín,Michael Shales,Pablo Fernandez-Piñar,Ping Wei,María Molina,Dorothea Fiedler,Kevan M. Shokat,Pedro Beltrao,Pedro Beltrao,Wendell A. Lim,Nevan J. Krogan +10 more
TL;DR: In this paper, a large-scale genetic interaction analysis in Saccharomyces cerevisiae involving approximately 49 × 1,200 double mutants in the presence of five different stress conditions, including osmotic, oxidative and cell wall-altering stresses.
Book ChapterDOI
The NIMA kinase: A mitotic regulator in Aspergillus nidulans and vertebrate cells
Kun Ping Lu,Tony Hunter +1 more
TL;DR: NIMA may represent a new essential eukaryotic cell cycle regulator, although its homologues in other species are yet to be identified.
Journal ArticleDOI
Constitutive activation of the Saccharomyces cerevisiae mating response pathway by a MAP kinase kinase from Candida albicans.
Karen L. Clark,Pascale J. F. Feldmann,Daniel Dignard,Robert Larocque,Alistair J. P. Brown,Melanie G. Lee,David Y. Thomas,Malcolm Whiteway +7 more
TL;DR: Creation of HST7/Ste7 hybrid proteins revealed that the C-terminal two-thirds of Hst7, which contains the protein kinase domain, is sufficient to confer this partial independence of upstream activators.
Journal ArticleDOI
Identification of residues in the cysteine-rich domain of Raf-1 that control Ras binding and Raf-1 activity.
David G. Winkler,Richard E. Cutler,Jonelle K. Drugan,Sharon L. Campbell,Deborah K. Morrison,Jonathan A. Cooper +5 more
TL;DR: It is proposed that a direct or indirect regulatory interaction between the N- and C-terminal regions of Raf-1 is reduced by the R143W, R143Q, and K144E mutations, thereby increasing access to the Ras-binding regions of Rafael-1 and increasing Raf- 1 activity.
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
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.
Journal ArticleDOI
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).
Journal ArticleDOI
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.
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.