Phosphorylation of the cap-binding protein eIF4E by the MAPK-activated protein kinase Mnk1.
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.
Pyronnet
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Department of Biochemistry, McGill University, Montreal, Quebec, Canada. Pyronnet@med.mcgill.ca
D002453:Cell Cycle / Q000502:physiology; D039561:Eukaryotic Initiation Factor-4E; D039603:Eukaryotic Initiation Factor-4G; D006801:Humans; D047908:Intracellular Signaling Peptides and Proteins; D010448:Peptide Initiation Factors / Q000378:metabolism* / Q000502:physiology; D010766:Phosphorylation; D011485:Protein Binding; D017346:Protein Serine-Threonine Kinases / Q000378:metabolism*; D039381:RNA Cap-Binding Proteins; D016601:RNA-Binding Proteins / Q000378:metabolism*
D039561:Eukaryotic Initiation Factor-4E; D039603:Eukaryotic Initiation Factor-4G; D047908:Intracellular Signaling Peptides and Proteins; D010448:Peptide Initiation Factors; D039381:RNA Cap-Binding Proteins; D016601:RNA-Binding Proteins; C491395:MKNK1 protein, human; D017346:Protein Serine-Threonine Kinases