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muscle ribosome synthesis functions as a nutrient-dependent checkpoint for overall body growth: in nutrient rich conditions, TOR is required to maintain levels of TIF-IA and ribosome synthesis to promote high levels of systemic insulin (show INS Proteins)
These data support a model in which activated Akt (show AKT1 Proteins) enhances rRNA synthesis both by preventing TIF-IA degradation and phosphorylating CK2alpha, which in turn phosphorylates TIF-IA.
DNA binding by the ribosomal DNA transcription factor rrn3 is essential for ribosomal DNA transcription
reveals the molecular basis of Rrn3-regulated Pol I initiation and cell growth
Data show that nutrient starvation, density arrest and protein synthesis inhibitors inactivate transcription initiation factor-IA and impair its association with RNA polymerase I (show POLR1C Proteins).
ERK (show EPHB2 Proteins)-dependent phosphorylation of the transcription initiation factor TIF-IA is required for RNA polymerase I (show POLR1C Proteins) transcription and cell growth.
Phosphorylation of S44 activates and S199 inactivates TIF-IA.
The definition of the Alu element within the TIF-IA gene as an exon is restricted to certain types of cancers; the element is not exonized in normal human cells.
CK2 phosphorylates the transcription initiation factor TIF-IA at serines 170 and 172 (Ser170/172), and this phosphorylation triggers the release of TIF-IA from Pol I after transcription initiation.
Conditional deletion of the Rrn3 gene inhibits RNA polymerase I (show POLR1C Proteins) transcription but does not affect pre-initiation complex formation.
The results exemplify how stress-induced inactivation of TIF-IA and long non-coding RNA -dependent changes of chromatin structure ensure repression of ribosomal RNA synthesis in response to thermo-stress.
Ablation of TIF-IA leads to impaired nucleolar activity and results in increased levels of the proapoptotic transcription factor p53 (show TP53 Proteins) in both neural progenitors and hippocampal neurons but induces rapid apoptosis only in neural progenitors.
Rrn3 regulates rDNA transcription by determining the steady-state concentration of the Rrn3.RNA polymerase I (show POLR1C Proteins) complex within the nucleolus. (RRN3)
Genetic inactivation of Tif1a (show TRIM24 Proteins) leads to nucleolar disruption, cell cycle arrest, and p53 (show TP53 Proteins)-mediated apoptosis.
Required for efficient transcription initiation by RNA polymerase I. Required for the formation of the competent preinitiation complex (PIC). Dissociates from pol I as a consequence of transcription. In vitro, cannot activate transcription in a subsequent transcription reaction.
RRN3 RNA polymerase I transcription factor homolog (S. cerevisiae)
, RRN3 RNA polymerase I transcription factor homolog
, RNA polymerase I-specific transcription initiation factor RRN3
, RNA polymerase I-specific transcription initiation factor RRN3-like
, transcription initiation factor IA
, transcription initiation factor TIF-IA