Epstein-Barr virus latent-infection membrane proteins are palmitoylated and raft-associated: Protein 1 binds to the cytoskeleton through TNF receptorcytoplasmic factors

Epstein-Barr virus encodes integral membrane proteins LMP1 and LMP2A in tra nsformed lymphoblastoid cell lines. We now find that LMP1 associates with t he cell cytoskeleton through a tumor necrosis factor receptor-associated fa ctor-interacting domain, most likely mediated by tumor necrosis factor rece ptor-associated factor 3. LMP1 is palmitoylated, and the transmembrane doma ins associate with lipid rafts. Mutation of LMP1 cysteine-78 abrogates palm itoylation but does not affect raft association or NF-kappaB or c-Jun N-ter minal kinase activation. LMP2A also associates with rafts and is palmitoyla ted but does not associate with the cell cytoskeleton. The associations of LMP1 and LMP2A with rafts and of LMP1 with the cell cytoskeleton are likely to effect interactions with cell proteins involved in shape, motility, sig nal transduction, growth, and survival.