Association of p300 and CBP with simian virus 40 large T antigen

Richard Eckner, John W. Ludlow, Nancy L. Lill, Elizabeth Oldread, Zoltan Arany, Nazanine Modjtahedi, James A. DeCaprio, David M. Livingston, Jeffery A. Morgan

Research output: Contribution to journalArticle

212 Scopus citations

Abstract

p300 and the CREB-binding protein CBP are two large nuclear phosphoproteins that are structurally highly related. Both function, in part, as transcriptional adapters and are targeted by the adenovirus E1A oncoprotein. We show here that p300 and CBP interact with another transforming protein, the simian virus 40 large T antigen (T). This interaction depends on the integrity of a region of T which is critical for its transforming and mitogenic properties and includes its LXCXE Rb-binding motif. T interferes with normal p300 and CBP function on at least two different levels. The presence of T alters the phosphorylation states of both proteins and inhibits their transcriptional activities on certain promoters. Although E1A and T show little sequence similarity, they interact with the same domain of p300 and CBP, suggesting that this region exhibits considerable flexibility in accommodating diverse protein ligands.

Original languageEnglish (US)
Pages (from-to)3454-3464
Number of pages11
JournalMolecular and cellular biology
Volume16
Issue number7
DOIs
StatePublished - Jan 1 1996

All Science Journal Classification (ASJC) codes

  • Molecular Biology
  • Cell Biology

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    Eckner, R., Ludlow, J. W., Lill, N. L., Oldread, E., Arany, Z., Modjtahedi, N., DeCaprio, J. A., Livingston, D. M., & Morgan, J. A. (1996). Association of p300 and CBP with simian virus 40 large T antigen. Molecular and cellular biology, 16(7), 3454-3464. https://doi.org/10.1128/MCB.16.7.3454