Rapamycin enhances eIF4E phosphorylation by activating MAP kinase-interacting kinase 2a (Mnk2a). (Q39129425)

9 September 2017

title

Rapamycin enhances eIF4E phosphorylation by activating MAP kinase-interacting kinase 2a (Mnk2a). (English)

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9 September 2017

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2

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9 September 2017

Rebecca L Stead

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9 September 2017

language of work or name

English

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publication date

4 July 2013

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9 September 2017

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9 September 2017

volume

587

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9 September 2017

issue

16

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9 September 2017

page(s)

2623-2628

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Targeting the eukaryotic translation initiation factor 4E for cancer therapy

9 September 2017

cites work

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The translation factor eIF-4E promotes tumor formation and cooperates with c-Myc in lymphomagenesis

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Active-site inhibitors of mTOR target rapamycin-resistant outputs of mTORC1 and mTORC2

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An ATP-competitive mammalian target of rapamycin inhibitor reveals rapamycin-resistant functions of mTORC1

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AZD8055 is a potent, selective, and orally bioavailable ATP-competitive mammalian target of rapamycin kinase inhibitor with in vitro and in vivo antitumor activity

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Mitogen-activated protein kinases activate the serine/threonine kinases Mnk1 and Mnk2

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MNK1, a new MAP kinase-activated protein kinase, isolated by a novel expression screening method for identifying protein kinase substrates

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The phosphorylation of eukaryotic initiation factor eIF4E in response to phorbol esters, cell stresses, and cytokines is mediated by distinct MAP kinase pathways

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Features of the catalytic domains and C termini of the MAPK signal-integrating kinases Mnk1 and Mnk2 determine their differing activities and regulatory properties

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The N and C termini of the splice variants of the human mitogen-activated protein kinase-interacting kinase Mnk2 determine activity and localization

21 January 2018

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https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2013.06.045

The mitogen-activated protein kinase signal-integrating kinase Mnk2 is a eukaryotic initiation factor 4E kinase with high levels of basal activity in mammalian cells

21 January 2018

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eIF4E phosphorylation promotes tumorigenesis and is associated with prostate cancer progression

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Combined deficiency for MAP kinase-interacting kinase 1 and 2 (Mnk1 and Mnk2) delays tumor development

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Dissecting eIF4E action in tumorigenesis

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Inhibition of mammalian target of rapamycin induces phosphatidylinositol 3-kinase-dependent and Mnk-mediated eukaryotic translation initiation factor 4E phosphorylation

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Retracted: Simultaneous Inhibition of mTOR-Containing Complex 1 (mTORC1) and MNK Induces Apoptosis of Cutaneous T-Cell Lymphoma (CTCL) Cells

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Phosphorylation of eIF4E by MNKs supports protein synthesis, cell cycle progression and proliferation in prostate cancer cells

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Activation of Akt and eIF4E survival pathways by rapamycin-mediated mammalian target of rapamycin inhibition.

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A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

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Human eukaryotic translation initiation factor 4G (eIF4G) recruits mnk1 to phosphorylate eIF4E

21 January 2018

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Mnk2 and Mnk1 are essential for constitutive and inducible phosphorylation of eukaryotic initiation factor 4E but not for cell growth or development

21 January 2018

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21 January 2018

Identifiers

DOI

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9 September 2017

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