NUCLEOTIDE SEQUENCE [MRNA] OF 13-427, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, INTERACTION WITH MAPK3; MAPK1 AND P38 KINASE, PHOSPHORYLATION AT THR-209 AND THR-214, MUTAGENESIS OF THR-209 AND THR-214
phosphorylation pattern of eIF4E responds faithfully to Rapamycin inhibition the prolonged exposure to Rapamycin rescues the loss of eIF4E phosphorylation through Mnk1 activation.
data suggest a physiological role for MNK1a-Ser(353) phosphorylation in regulation of the MNK1a kinase which correlates with increased eIF4E phosphorylation in vitro and in vivo.
MNK1 participates in mediating high-fat diet-induced insulin resistance. Our findings reveal distinct roles for the MNKs in a novel area of disease biology
Data suggest that Mnk1 and Mnk2 regulate cell migration/wound healing expression of vimentin stability of vimentin protein and binding of eIF4E (eukaryotic translation initiation factor 4E) and Cyfip1 (cytoplasmic FMR1 interacting protein 1).
Long-term potentiation (LTP) consolidation in the dentate gyrus of live rodents requires sustained (hours) BDNF-TrkB signaling and from TrkB to MAP-kinase-interacting kinase.
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