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. 1996 Oct 1;93(20):10626–10631. doi: 10.1073/pnas.93.20.10626

The nuclear hormone receptor coactivator SRC-1 is a specific target of p300.

T P Yao 1, G Ku 1, N Zhou 1, R Scully 1, D M Livingston 1
PMCID: PMC38204  PMID: 8855229

Abstract

p300 and its family member, CREB-binding protein (CBP), function as key transcriptional coactivators by virtue of their interaction with the activated forms of certain transcription factors. In a search for additional cellular targets of p300/CBP, a protein-protein cloning strategy, surprisingly identified SRC-1, a coactivator involved in nuclear hormone receptor transcriptional activity, as a p300/CBP interactive protein. p300 and SRC-1 interact, specifically, in vitro and they also form complexes in vivo. Moreover, we show that SRC-1 encodes a new member of the basic helix-loop-helix-PAS domain family and that it physically interacts with the retinoic acid receptor in response to hormone binding. Together, these results implicate p300 as a component of the retinoic acid signaling pathway, operating, in part, through specific interaction with a nuclear hormone receptor coactivator, SRC-1.

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