Identification of p100 as a coactivator for STAT6 that bridges STAT6 with RNA polymerase II.

STAT6 is a central mediator of IL-4-induced gene responses. STAT6-mediated transcription is depend ent on the C-terminal transcription activation domain (TAD), but the mechanisms by which STAT6 activates transcription are poorly understood. Here, we have identified the staphylococcal nuclease (SN)-like domain and tudor domain containing protein p100 as a STAT6 ...
TAD interacting protein. p100 was originally characterized as a transcriptional coactivator for Epstein-Barr virus nuclear antigen 2. STAT6 interacted with p100 in vitro and in vivo. The interaction was mediated by the TAD domain of STAT6 and the SN-like domain of p100. p100 did not affect the immediate activation events of STAT6, but enhanced STAT6-mediated transcriptional activation and the IL-4-induced Igepsilon gene transcription in human B-cell line. Finally, p100 associated with the large subunit of RNA polymerase II and was mediating interaction between STAT6 and RNA polymerase II. These findings identify p100 as a novel coactivator for STAT6 and suggest that p100 functions as a bridging factor between STAT6 and the basal transcription machinery.
Mesh Terms:
Animals, Cell Fractionation, Cell Line, Genes, Reporter, Humans, Immunoglobulin E, Interleukin-4, Nuclear Proteins, Protein Structure, Tertiary, RNA Polymerase II, Recombinant Fusion Proteins, STAT6 Transcription Factor, Signal Transduction, Trans-Activators, Transcription, Genetic
EMBO J.
Date: Sep. 16, 2002
Download Curated Data For This Publication
10484
Switch View:
  • Interactions 6