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Data show that galeterone (gal (show GAL Proteins)) and VNPT55 inhibit migration and invasion of prostate cancer cells, possibly by down-regulating protein expression via antagonizing the Mnk1 (show MKNK1 Proteins)/2-eIF4E (show EIF4E Proteins) axis.
Data suggest MNK1 (show MKNK1 Proteins)/MNK2 stimulate mRNA translation but only of mRNA containing both 5-prime-terminal cap and hairpin duplex; this stimulation involves up-regulation of phosphorylation/mRNA un-winding activity of eIF4E (show EIF4E Proteins) (via decreased binding to eIF4G (show EIF4G1 Proteins)).
MNK1 (show MKNK1 Proteins) and MNK2 inhibition ablates eIF4E1 (show EIF4E Proteins) phosphorylation and concurrently enhances eIF4E3 (show EIF4E3 Proteins) expression in diffuse large B-cell lymphoma.
Data show that interferon-gamma (show IFNG Proteins) regulated the metabolism and mRNA translation of macrophages by targeting the kinases mTORC1 and MNK1 (show MKNK1 Proteins)/2, both of which converge on the selective regulator of translation initiation eukaryotic initiation factor-4E (eIF4E (show EIF4E Proteins)).
Provide evidence for the existence of a Mnk2/eIF4E (show EIF4E Proteins)-controlled feedback loop in medulloblastoma cells that accounts for resistance to mTORC1 inhibitors.
Data suggest that a combined pharmacologic inhibition of mTORC1 and Mnk1/2 kinases offers a therapeutic opportunity in blast crisis-chronic myeloid leukemia (BC-CML).
These findings provide evidence for key and essential roles of the Mnk kinase pathway in the generation of the antineoplastic effects of type I IFNs in Jak2V617F-dependent myeloproliferative neoplasms.
eIF4E (show EIF4E Proteins) phosphorylation is enhanced by Rapamycin, which activates Mnk2a
MNK2-dependent phosphorylation of eIF4E (show EIF4E Proteins) represents a novel drug resistance, pro-survival pathway in pancreatic ductal carcinoma.
siRNA-mediated Mnk1 (show MKNK1 Proteins)/2 knockdown results in partial reversal of the suppressive effects of IFNgamma on human CD34 (show CD34 Proteins)+-derived myeloid (CFU-GM) and erythroid (BFU-E) progenitors.
Data suggest that Mnk1 (show MKNK1 Proteins) and Mnk2 regulate cell migration/wound healing, expression of vimentin (show VIM Proteins), stability of vimentin (show VIM Proteins) protein, and binding of eIF4E (eukaryotic translation initiation factor 4E (show EIF4E Proteins)) and Cyfip1 (cytoplasmic FMR1 interacting protein 1 (show CYFIP1 Proteins)).
Mnk2a directly interacts with and translocates p38alpha (show MAPK14 Proteins)-MAPK (show MAPK1 Proteins) into the nucleus. Alternatively, Mnk2b does not activate p38-MAPK (show MAPK14 Proteins).
Mnk1 (show MKNK1 Proteins)/2 has a minimal role in T cell development and activation but may regulate non-T cell lineages to control Th1 (show HAND1 Proteins) and Th17 differentiation in vivo.
Data indicate that MNK2 plays a unique role, not shared by its closest paralog MNK1 (show MKNK1 Proteins), in limiting protein translation through its negative effect on eIF4G (show EIF4G1 Proteins) Ser1108 phosphorylation and p70S6K (show RPS6KB1 Proteins) activation.
MAP kinase (show MAPK1 Proteins)-interacting kinase 1 and 2 activity enhances formation of the EIF-4F complex in pachytene spermatocytes but not in round spermatids.
oncogenic role for Mnk1 (show MKNK1 Proteins)/2 in tumor development
Mnk2 and Mnk1 (show MKNK1 Proteins) are essential for constitutive and inducible phosphorylation of eukaryotic initiation factor 4E (show EIF4EBP2 Proteins) but not for cell growth or development
The roles of features in the catalytic domains and C termini in determining the regulatory properties and basal activities of Mnk1 (show MKNK1 Proteins) AND Mnk2 are reported.
Roles of mitogen-activated protein kinase (show MAPK1 Proteins) signal-integrating kinases 1 and 2 in oxidant-mediated eIF4E (show EIF4E Proteins) phosphorylation.
This gene encodes a member of the calcium/calmodulin-dependent protein kinases (CAMK) Ser/Thr protein kinase family, which belongs to the protein kinase superfamily. This protein contains conserved DLG (asp-leu-gly) and ENIL (glu-asn-ile-leu) motifs, and an N-terminal polybasic region which binds importin A and the translation factor scaffold protein eukaryotic initiation factor 4G (eIF4G). This protein is one of the downstream kinases activated by mitogen-activated protein (MAP) kinases. It phosphorylates the eukaryotic initiation factor 4E (eIF4E), thus playing important roles in the initiation of mRNA translation, oncogenic transformation and malignant cell proliferation. In addition to eIF4E, this protein also interacts with von Hippel-Lindau tumor suppressor (VHL), ring-box 1 (Rbx1) and Cullin2 (Cul2), which are all components of the CBC(VHL) ubiquitin ligase E3 complex. Multiple alternatively spliced transcript variants have been found, but the full-length nature and biological activity of only two variants are determined. These two variants encode distinct isoforms which differ in activity and regulation, and in subcellular localization.
MAP kinase interacting serine/threonine kinase 2
, MAP kinase-interacting serine/threonine kinase 2
, MAP kinase signal-integrating kinase 2
, MAP kinase-interacting serine/threonine-protein kinase 2
, MAPK signal-integrating kinase 2
, G protein-coupled receptor kinase 7