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. 2012 May;86(9):5179–5191. doi: 10.1128/JVI.00169-12

Fig 4.

Fig 4

LANA interacts with PP2A. (A) LANA interacts with the B′ subunit of PP2A. Cell extract from HEK 293T cells transfected with expression vectors for Flag-LANA and HA-PP2A A, B′, or C subunits were immunoprecipitated with anti-Flag-conjugated beads. (B) LANA interacts with endogenous A and B but not C PP2A subunits. Extracts of Flag-LANA-transfected HEK 293T cells were immunoprecipitated with anti-Flag-conjugated beads and subjected to SDS-PAGE and Western blot analysis. Specific antibodies against PP2A B (top), PP2A A (second from top), and PP2A C (second from bottom) were used to detect endogenous PP2A proteins. Expression of LANA was detected with anti-LANA antibody (bottom). (C) LANA does not globally disrupt the PP2A complex. HEK 293T cells were transfected with expression vectors for HA-PP2A B′ and LANA. Total cell extracts were immunoprecipitated with anti-HA-conjugated beads and subjected to SDS-PAGE and Western blot analysis. Coimmunoprecipitated (top) and input (second from top) endogenous PP2A C were detected with anti-PP2A C antibody. (D) LANA does not globally disrupt the nuclear PP2A complex. HEK 293T cells were transfected with expression vectors for HA-PP2A C and LANA. Nuclear extracts were immunoprecipitated with anti-HA-conjugated beads and subjected to SDS-PAGE and Western blot analysis. Coimmunoprecipitated endogenous PP2A A and B were detected with anti-PP2A A and PP2A B antibodies, respectively.