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

被引:38
作者
Barth-Baus, D
Stratton, CA
Parrott, L
Myerson, H
Meyuhas, O
Templeton, DJ
Landreth, GE
Hensold, JO
机构
[1] Case Western Reserve Univ, Sch Med, Dept Neurosci, Cleveland, OH 44106 USA
[2] Case Western Reserve Univ, Ireland Canc Ctr, Cleveland, OH 44106 USA
[3] Case Western Reserve Univ, Sch Med, Dept Med, Cleveland, OH 44106 USA
[4] Case Western Reserve Univ, Sch Med, Cleveland Vet Affairs Med Ctr, Cleveland, OH 44106 USA
[5] Case Western Reserve Univ, Sch Med, Inst Pathol, Cleveland, OH 44106 USA
[6] Hebrew Univ Jerusalem, Hadassah Med Sch, IL-91010 Jerusalem, Israel
关键词
D O I
10.1093/nar/30.9.1919
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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 downstream 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.
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页码:1919 / 1928
页数:10
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