mTOR-dependent activation of the transcription factor TIF-IA links rRNA synthesis to nutrient availability.

In cycling cells, transcription of ribosomal RNA genes by RNA polymerase I (Pol I) is tightly coordinated with cell growth. Here, we show that the mammalian target of rapamycin (mTOR) regulates Pol I transcription by modulating the activity of TIF-IA, a regulatory factor that senses nutrient and growth-factor availability. Inhibition ...
of mTOR signaling by rapamycin inactivates TIF-IA and impairs transcription-initiation complex formation. Moreover, rapamycin treatment leads to translocation of TIF-IA into the cytoplasm. Rapamycin-mediated inactivation of TIF-IA is caused by hypophosphorylation of Se 44 (S44) and hyperphosphorylation of Se 199 (S199). Phosphorylation at these sites affects TIF-IA activity in opposite ways, for example, phosphorylation of S44 activates and S199 inactivates TIF-IA. The results identify a new target formTOR-signaling pathways and elucidate the molecular mechanism underlying mTOR-dependent regulation of RNA synthesis.
Mesh Terms:
3T3 Cells, Amino Acid Substitution, Animals, Cell Division, Cell Line, Cell Nucleus, Humans, Mice, Mutagenesis, Site-Directed, Nucleic Acid Hybridization, Phosphates, Phosphorylation, Pol1 Transcription Initiation Complex Proteins, Protein Kinases, Protein Transport, RNA Polymerase I, RNA, Ribosomal, Signal Transduction, Sirolimus, Transcription Factors, Transcription, Genetic
Genes Dev.
Date: Feb. 15, 2004
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