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In ovarian granulosa cells, FHL2 was found to be a coactivator of NR5A nuclear receptors [ 16].
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This protein has been found to be a coactivator involved in regulated transcription of RNA polymerase II-dependent genes important in transcription and other regulatory mechanisms [ 30].
Paradoxically, MTA1 was also found to be a coactivator protein [ 102].
Originally discovered because of its ability to target p53 for degradation by the proteosome in association with the human papillomavirus E6 protein [ 48], E6-associated protein (E6-AP) was later found to be a nuclear hormone receptor coactivator [ 49].
Furthermore, ANKRD11 was found to be a novel p53-interacting protein enhancing the transcriptional activity of p53, hence functioning as a p53 coactivator.
Since its identification as a c-Jun coactivator [ 1], Jab1 has been found to be an integral component of the COP9 signalosome (CSN) complex, a multifunctional protein complex involved in modulating signal transduction, gene transcription, and protein stability [ 2- 4].
Moreover, HIF-1 α was revealed to be a coactivator of estrogen-dependent VEGF synthesis [ 26].
Additionally, GREB1 has been demonstrated to be a coactivator of estrogen receptor-α [ 45].
Recruitment of both SRC-1 and SRC-3 was found to be dependent on p300, which suggests a central coactivator role for p300.
Furthermore, Fgf21 was shown to mediate its effect partly via upregulation of Ppargc1a[ 27], a transcriptional coactivator we found to be highly increased by fasting in accordance with Fgf21 levels.
Unconventional transcriptional coactivators like the XPC complex and YAP are often found to be multifunctional.
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