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. 2019 Jan 28;15(1):e1007543. doi: 10.1371/journal.ppat.1007543

Fig 6. MCPyV LT-t and ST do not interact with the E3 ubiquitin ligase Fbw1 (β-TrCP).

Fig 6

(A) Fbw1, was assessed for its ability to co-immunoprecipitate MCPyV T antigens. 293A cells co-transfected with individual or combinations of Fbw7 (4.5μg), Fbw1 (3μg), MCPyV LT (5μg), MCPyV LT-t (10.5μg), or MCPyV ST (1μg). MCPyV T antigens were pulled down with XT10, and Fbw7 or Fbw1 co-immunoprecipitation was detected by immunoblotting with anti-FLAG. (B) A mutation in the proposed Fbw1 binding domain of MCPyV LT-t, S147A, was also assessed for its ability to co-immunoprecipitate Fbw1. (C and D) MCPyV LT and LT-t were immunoprecipitated with XT10 and stained for co-immunopreciptated Fbw7, Fbw1, ΔFbox, or WD40 (Fbw1ARG) mutants (FLAG).