S6 phosphorylation-independent pathways regulate translation of 5′-terminal oligopyrimidine tract-containing mRNAs in differentiating hematopoietic cells

Diane Barth-Baus, Carl A. Stratton, Lou Parrott, Howard Myerson, Oded Meyuhas, Dennis J. Templeton, Gary E. Landreth, Jack O. Hensold*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

40 Scopus citations

Abstract

Synthesis of new ribosomes is an energy costly and thus highly regulated process. Ribosomal protein synthesis is controlled by regulating translation of the corresponding ribosomal protein (rp)mRNAs. In mammalian cells a 5′-terminal oligopyrimidine tract (TOP) is a conserved feature of these mRNAs that has been demonstrated to be essential for their translational regulation. Translation of TOP mRNAs has been proposed to be regulated by phosphorylation of ribosomal protein S6, which is a common effect of mitogenic stimulation of cells. However, as demonstrated here, S6 phosphorylation is not detectable in murine erythroleukemia (MEL) or other hematopoietic cells. The absence of S6 phosphorylation appears to be due to the action of a phosphatase that acts down-stream of S6 kinase, presumably on S6 itself. Despite the absence of changes in S6 phosphorylation, translation of TOP mRNAs is repressed during differentiation of MEL cells. These data demonstrate the existence of a mechanism for regulating S6 phosphorylation that is distinct from kinase activation, as well as the existence of mechanisms for regulating translation of TOP mRNAs that are independent of S6 phosphorylation.

Original languageEnglish
Pages (from-to)1919-1928
Number of pages10
JournalNucleic Acids Research
Volume30
Issue number9
DOIs
StatePublished - 1 May 2002

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