Proposed model of the role of Hsp72 and CHIP in EBNALP coactivation of EBNA2-mediated transcription. Hsp72 stably associates with EBNALP and chaperones EBNALP through transient interaction with EBNA2 and more stable interactions with Sp100, HDAC4, and HP1α repressor complexes.^4,25,59  EBNALP shuttles Sp100, HDAC4, and HP1α from EBNA2-responsive promoters to other nuclear or cytoplasmic locations,^4,59  and thereby coactivates with EBNA2 in enabling RNA polymerase II complex assembly and transcription. CHIP can downmodulate the Hsp72 effect on EBNALP coactivation with EBNA2, but also can have a positive effect on EBNA2 in the absence of EBNALP.