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Molecular and Cellular Biology, March 1999, p. 1871-1880, Vol. 19, No. 3
0270-7306/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Phosphorylation of the Cap-Binding Protein Eukaryotic Translation Initiation Factor 4E by Protein Kinase Mnk1 In Vivo

Andrew Jan Waskiewicz,1 Jeffrey C. Johnson,1 Bennett Penn,1,2 Malathy Mahalingam,1 Scot R. Kimball,3 and Jonathan A. Cooper1,*

Fred Hutchinson Cancer Research Center, Seattle, Washington 981091; Medical Scientist Training Program, University of Washington, Seattle, Washington 981952; and Department of Cellular and Molecular Physiology, The Pennsylvania State University College of Medicine, Hershey Medical Center, Hershey, Pennsylvania 170333

Received 13 August 1998/Returned for modification 15 September 1998/Accepted 25 November 1998

Eukaryotic translation initiation factor 4E (eIF4E) binds to the mRNA 5' cap and brings the mRNA into a complex with other protein synthesis initiation factors and ribosomes. The activity of mammalian eIF4E is important for the translation of capped mRNAs and is thought to be regulated by two mechanisms. First, eIF4E is sequestered by binding proteins, such as 4EBP1, in quiescent cells. Mitogens induce the release of eIF4E by stimulating the phosphorylation of 4EBP1. Second, mitogens and stresses induce the phosphorylation of eIF4E at Ser 209, increasing the affinity of eIF4E for capped mRNA and for an associated scaffolding protein, eIF4G. We previously showed that a mitogen- and stress-activated kinase, Mnk1, phosphorylates eIF4E in vitro at the physiological site. Here we show that Mnk1 regulates eIF4E phosphorylation in vivo. Mnk1 binds directly to eIF4G and copurifies with eIF4G and eIF4E. We identified activating phosphorylation sites in Mnk1 and developed dominant-negative and activated mutants. Expression of dominant-negative Mnk1 reduces mitogen-induced eIF4E phosphorylation, while expression of activated Mnk1 increases basal eIF4E phosphorylation. Activated mutant Mnk1 also induces extensive phosphorylation of eIF4E in cells overexpressing 4EBP1. This suggests that phosphorylation of eIF4E is catalyzed by Mnk1 or a very similar kinase in cells and is independent of other mitogenic signals that release eIF4E from 4EBP1.

* Corresponding author. Mailing address: Fred Hutchinson Cancer Research Center, A2-025, 1100 Fairview Ave. North, Seattle, WA 98109. Phone: (206) 667-4454. Fax: (206) 667-6522. E-mail: jcooper{at}fhcrc.org.

Molecular and Cellular Biology, March 1999, p. 1871-1880, Vol. 19, No. 3
0270-7306/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


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