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

T P Yao1, G Ku, N Zhou

  • 1Dana-Farber Cancer Institute, Boston, MA, USA.

Proceedings of the National Academy of Sciences of the United States of America
|October 1, 1996
PubMed

Insights

p300 and CREB-binding protein (CBP) are transcriptional coactivators. Researchers discovered SRC-1 interacts with p300/CBP, implicating p300 in the retinoic acid signaling pathway via SRC-1.

Area of Science:

  • Molecular Biology
  • Gene Regulation
  • Protein Interactions

Background:

  • p300 and CREB-binding protein (CBP) are crucial transcriptional coactivators.
  • They function by interacting with activated transcription factors.
  • Identifying additional cellular targets of p300/CBP is important for understanding gene regulation.

Purpose of the Study:

  • To identify novel cellular targets of p300/CBP.
  • To investigate the interaction between p300/CBP and other coactivators.
  • To elucidate the role of p300 in nuclear hormone receptor signaling pathways.

Main Methods:

  • Protein-protein interaction cloning strategy was employed.
  • In vitro and in vivo interaction studies were conducted.
  • SRC-1's role in nuclear hormone receptor activity was examined.

Main Results:

  • SRC-1, a nuclear hormone receptor coactivator, was identified as a p300/CBP interactive protein.
  • p300 and SRC-1 were shown to interact specifically both in vitro and in vivo.
  • SRC-1 was found to encode a new member of the basic helix-loop-helix-PAS domain family.
  • SRC-1 physically interacts with the retinoic acid receptor upon hormone binding.

Conclusions:

  • p300 interacts with SRC-1, a nuclear hormone receptor coactivator.
  • These findings implicate p300 as a component of the retinoic acid signaling pathway.
  • The interaction between p300 and SRC-1 is a key mechanism in this pathway.

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