Phosphorylation of the cap-binding protein eIF4E by the MAPK-activated protein kinase Mnk1
S Pyronnet - Biochemical pharmacology, 2000 - Elsevier
S Pyronnet
Biochemical pharmacology, 2000•ElsevierThe purpose of this review is to summarize recent experimental data describing the
regulation of the phosphorylation of eIF4E, the cap-binding protein, by the MAPK-activated
protein kinase Mnk1. Mnk1 does not interact directly with eIF4E, but uses a docking site in
eIF4G, a partner of eIF4E. Consequently, control of eIF4E phosphorylation may not strictly
depend on changes in Mnk1 activity. The possibility that integrity of the eIF4E/eIF4G/Mnk1
complex also impinges upon eIF4E phosphorylation is discussed.
regulation of the phosphorylation of eIF4E, the cap-binding protein, by the MAPK-activated
protein kinase Mnk1. Mnk1 does not interact directly with eIF4E, but uses a docking site in
eIF4G, a partner of eIF4E. Consequently, control of eIF4E phosphorylation may not strictly
depend on changes in Mnk1 activity. The possibility that integrity of the eIF4E/eIF4G/Mnk1
complex also impinges upon eIF4E phosphorylation is discussed.
The purpose of this review is to summarize recent experimental data describing the regulation of the phosphorylation of eIF4E, the cap-binding protein, by the MAPK-activated protein kinase Mnk1. Mnk1 does not interact directly with eIF4E, but uses a docking site in eIF4G, a partner of eIF4E. Consequently, control of eIF4E phosphorylation may not strictly depend on changes in Mnk1 activity. The possibility that integrity of the eIF4E/eIF4G/Mnk1 complex also impinges upon eIF4E phosphorylation is discussed.
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