Association of p300 and CBP with simian virus 40 large T antigen.
AUTOR(ES)
Eckner, R
RESUMO
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.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=231340Documentos Relacionados
- p300 family members associate with the carboxyl terminus of simian virus 40 large tumor antigen.
- Association of insulin receptor substrate 1 with simian virus 40 large T antigen.
- p53 Targets Simian Virus 40 Large T Antigen for Acetylation by CBP
- The zinc finger region of simian virus 40 large T antigen.
- Detection and characterization of multiple forms of simian virus 40 large T antigen.