Yao T P, Ku G, Zhou N, Scully R, Livingston D M
Dana-Farber Cancer Institute, Boston, MA, USA.
Proc Natl Acad Sci U S A. 1996 Oct 1;93(20):10626-31. doi: 10.1073/pnas.93.20.10626.
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.
p300及其家族成员——CREB结合蛋白（CBP），通过与某些转录因子的激活形式相互作用，发挥关键转录共激活因子的功能。在寻找p300/CBP的其他细胞靶点时，一种蛋白质-蛋白质克隆策略意外地鉴定出SRC-1，一种参与核激素受体转录活性的共激活因子，作为p300/CBP相互作用蛋白。p300和SRC-1在体外特异性相互作用，在体内也形成复合物。此外，我们表明SRC-1编码基本螺旋-环-螺旋-PAS结构域家族的一个新成员，并且它在激素结合后与视黄酸受体发生物理相互作用。这些结果共同表明p300是视黄酸信号通路的一个组成部分，部分通过与核激素受体共激活因子SRC-1的特异性相互作用发挥作用。
