B. Belandia et Mg. Parker, Functional interaction between the p160 coactivator proteins and the transcriptional enhancer factor family of transcription factors, J BIOL CHEM, 275(40), 2000, pp. 30801-30805
SRC1, initially identified as a nuclear receptor coactivator, was found to
interact with a member of the transcriptional enhancer factor (TEF) family
of transcription factors, TEF-4, The interaction, which occurs in both inta
ct cells and in a cell-free system, is mediated by the highly conserved bas
ic helix-loop-helix/Per-Arnt-Sim (bHLH-PAS) domain present in the N-termina
l region of SRC1. Moreover, all three members of the p160 family of nuclear
receptor coactivators, SRC1, TIF2, and RAGS, are able to potentiate transc
ription from a TEF response element in transient transfection experiments,
and this activation requires the presence of the bHLH-PAS domain. These res
ults suggest that the p160 proteins could be bona fide coactivators of the
TEF family of transcription factors.