Disease relevance of Ep400

• Several cellular polypeptides critical for growth regulation interact with DNA tumor virus oncoproteins. p400 is a cellular protein which binds to the adenovirus E1A oncoprotein(s) [1].
• Like p300, p400 is a phosphoprotein that binds to the simian virus 40 large tumor antigen (T) [1].
• Integration and amplification of ecotropic and recombinant proviral sequences in high-molecular-weight cellular DNAs from ecotropic Gross virus-accelerated AKR thymomas were analyzed using an ecotropic-specific probe, p400, and an envelope-specific probe, pAKV-5 [2].

High impact information on Ep400

• Therefore, whereas E1A inactivates the retinoblastoma protein, it requires p400 to efficiently promote cell death [3].
• These results identify p400 as a regulator of the ARF-p53 pathway and a component of the cellular machinery that couples proliferation to cell death [3].
• p400 is required for E1A to promote apoptosis [3].
• This was further supported by the tissue distribution observed only in yolk sac, kidney, and ileum with monospecific antiserum for p400 [4].
• A T species composed of residues 251 to 708 bound both p400 and p300, while a T species defective in p53 binding was unable to bind either detectably [1].

Biological context of Ep400

• Expression of the mDomino Q-rich domain, together with MZF-2A in myeloid LGM-1 cells, enhanced the MZF-2A-mediated activation of a reporter gene [5].
• CONCLUSIONS: These results strongly suggest that an ATP-dependent chromatin-remodelling complex containing mDomino interacts with MZF-2A to regulate gene expression in myeloid cells [5].

Analytical, diagnostic and therapeutic context of Ep400

• The principal protein, p400, had an M(r) of 400,000 in SDS-PAGE [4].

References