Phosphorylation of Mnk1 by caspase-activated Pak2/gamma-PAK inhibits phosphorylation and interaction of eIF4G with Mnk (Q28270295)

1

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Jun Ling

2

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Andrew J Waskiewicz

3

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Jonathan A Cooper

4

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William C Merrick

5

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Nadejda L Korneeva

6

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Robert E Rhoads

7

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Jolinda A Traugh

Journal of Biological Chemistry

9

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language of work or name

English

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publication date

10 September 2004

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published in

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volume

279

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page(s)

38649-57

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issue

37

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cites work

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Regulation of translation initiation factors by signal transduction.

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Phosphorylation of eIF-4E on serine 209 by protein kinase C is inhibited by the translational repressors, 4E-binding proteins

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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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Phosphorylation of the cap-binding protein eukaryotic translation initiation factor 4E by protein kinase Mnk1 in vivo

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Translational regulation during activation of porcine peripheral blood lymphocytes: association and phosphorylation of the alpha and gamma subunits of the initiation factor complex eIF-4F.

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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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Serum-stimulated, rapamycin-sensitive phosphorylation sites in the eukaryotic translation initiation factor 4GI.

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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

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

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p21-activated Protein Kinase γ-PAK Is Activated by Ionizing Radiation and Other DNA-damaging Agents

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Cytostatic p21 G protein-activated protein kinase gamma-PAK

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Activation of hPAK65 by caspase cleavage induces some of the morphological and biochemical changes of apoptosis

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Caspase-activated PAK-2 is regulated by subcellular targeting and proteasomal degradation

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Phosphorylation of elongation factor 1 and ribosomal protein S6 by multipotential S6 kinase and insulin stimulation of translational elongation

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Insulin stimulation of phosphorylation of elongation factor 1 (eEF-1) enhances elongation activity

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Caspase cleavage of initiation factor 4E-binding protein 1 yields a dominant inhibitor of cap-dependent translation and reveals a novel regulatory motif

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Features in the N and C termini of the MAPK-interacting kinase Mnk1 mediate its nucleocytoplasmic shuttling

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Internal ribosome initiation of translation and the control of cell death.

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release_355zucc2vbda3kiso7a43ypcuq

21 January 2018

Identifiers

DOI

10.1074/JBC.M407337200

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Fatcat ID

1 reference

Fatcat

https://api.fatcat.wiki/v0/release/355zucc2vbda3kiso7a43ypcuq