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Molecular and Cellular Biology, January 2006, p. 277-292, Vol. 26, No. 1
0270-7306/06/$08.00+0     doi:10.1128/MCB.26.1.277-292.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Akt-Mediated YB-1 Phosphorylation Activates Translation of Silent mRNA Species

Departments of Pathology and Pediatrics, British Columbia Research Institute for Children's and Women's Health, and University of British Columbia, 950 West 28th Avenue, Vancouver, BC, Canada V5Z 4H4,¹ Genome Sciences Centre, 600 West 10th Avenue, Vancouver, BC, Canada V5Z 4E6,² Institute of Protein Research, Pushchino, Moscow Region 142290, Russian Federation,³ Department of Pathology and Laboratory Medicine, Children's Hospital Los Angeles, 4650 Sunset Boulevard, Los Angeles, California 90027,⁴ Department of Biochemistry, McGill University, 3655 Promenade Sir William Osler, Montreal, Quebec, Canada H3G 1Y6⁵

Received 23 June 2005/ Returned for modification 28 July 2005/ Accepted 3 October 2005

YB-1 is a broad-specificity RNA-binding protein that is involved in regulation of mRNA transcription, splicing, translation, and stability. In both germinal and somatic cells, YB-1 and related proteins are major components of translationally inactive messenger ribonucleoprotein particles (mRNPs) and are mainly responsible for storage of mRNAs in a silent state. However, mechanisms regulating the repressor activity of YB-1 are not well understood. Here we demonstrate that association of YB-1 with the capped 5' terminus of the mRNA is regulated via phosphorylation by the serine/threonine protein kinase Akt. In contrast to its nonphosphorylated form, phosphorylated YB-1 fails to inhibit cap-dependent but not internal ribosome entry site-dependent translation of a reporter mRNA in vitro. We also show that similar to YB-1, Akt is associated with inactive mRNPs and that activated Akt may relieve translational repression of the YB-1-bound mRNAs. Using Affymetrix microarrays, we found that many of the YB-1-associated messages encode stress- and growth-related proteins, raising the intriguing possibility that Akt-mediated YB-1 phosphorylation could, in part, increase production of proteins regulating cell proliferation, oncogenic transformation, and stress response.

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