Phosphorylation of the cap-binding protein eIF4E by the MAPK-activated protein kinase Mnk1

• Published in: Biochemical pharmacology Vol. 60; no. 8; pp. 1237 - 1243
• Main Author: Pyronnet, Stéphane
• Format: Journal Article Conference Proceeding
• Language: English
• Published: New York, NY Elsevier Inc 15.10.2000; Elsevier Science
• Subjects: Biological and medical sciences; cap binding protein; cell cycle; Cell Cycle - physiology; Cell physiology; Eukaryotic Initiation Factor-4E; Eukaryotic Initiation Factor-4G; Fundamental and applied biological sciences. Psychology; Humans; Intracellular Signaling Peptides and Proteins; Mnk1; Molecular and cellular biology; Molecular genetics; Peptide Initiation Factors - metabolism; Peptide Initiation Factors - physiology; Phosphorylation; Protein Binding; Protein-Serine-Threonine Kinases - metabolism; RNA Cap-Binding Proteins; RNA-Binding Proteins - metabolism; Signal transduction; translation initiation; Translation. Translation factors. Protein processing; translation initiation; Mnk1; cap binding protein; cell cycle; phosphorylation; Binding protein; Signal transduction; Phosphorylation; Enzyme; Protein kinase; Transferases; Cap structure; Initiation factor eIF4E; Cell cycle; Translation initiation; Review
• ISSN: 0006-2952; 1873-2968
• DOI: 10.1016/S0006-2952(00)00429-9

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.