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. 2002 Apr;22(7):2136–2146. doi: 10.1128/MCB.22.7.2136-2146.2002

FIG. 8.

FIG. 8.

Schematic model for the role of HA95 and PKA in EBNA-LP coactivation with EBNA-2 of the EBV LMP1 latency promoter. EBNA-2 can multimerize through two self-associating N-terminal domains (25). EBNA-2 then binds to specific viral and cell promoters through interaction with RBP-Jκ and PU.1 (for a review see reference 34). The EBNA-2 acidic domain mediates transcriptional activation through interactions with p100 (66), TFIIH (65), TFIIB (67), p300/CBP (74), and EBNA-LP (24). The p100 protein is a scaffold for c-Myb (9) and Pim-1 (37). The data herein indicate that the EBNA-LP repeat domain is complexed with HA95. EBNA-LP and HA95 can each self associate (43, 48). HA95 was previously known to be associated with RHA (75, 77). RHA is part of a Pol II holoenzyme complex that includes CBP/p300, BRCA1, and Pol II (3, 38, 46, 77). In recruiting RHA and its associated CBP/p300, BRCA1, and Pol II proteins, HA95 should have positive transcriptional effects. In recruiting PKAcsα, HA95 has negative direct effects on EBNA-LP-mediated coactivation with EBNA-2. PKAcsα may also have positive effects through HA95 by an effect on CREB mediated by CBP that is associated with HA95 through RHA.