American Society of Hematology

Figure 4.

$Increased interaction of RelB with mutant E418X, R635X in nuclear fraction. HEK293T cells were transiently transfected with the indicated constructs in the presence and absence of NIK coexpression. (A) Cytoplasmic and (B) nuclear fractions were prepared, and immunoprecipitated with an α-HA antibody. Cell lysates from IP samples were analyzed for the interaction of NF-κB2 (WT or mutants) with RelB. The faint band at 50 kDa in all lanes is immunoglobulin heavy chain. Immunoblotting of Lamin A/C and GAPDH was used as a marker for the nuclear and cytoplasmic fraction, respectively. Red asterisks indicate increased interaction of mutant E418X, R635X with RelB without NIK expression. Blue asterisks indicate increased translocation of mutant forms E418X, R635X, and active form of NF-κB2 (p52) to the nucleus. Data shown are representative of 3 experiments.$

Increased interaction of RelB with mutant E418X, R635X in nuclear fraction. HEK293T cells were transiently transfected with the indicated constructs in the presence and absence of NIK coexpression. (A) Cytoplasmic and (B) nuclear fractions were prepared, and immunoprecipitated with an α-HA antibody. Cell lysates from IP samples were analyzed for the interaction of NF-κB2 (WT or mutants) with RelB. The faint band at 50 kDa in all lanes is immunoglobulin heavy chain. Immunoblotting of Lamin A/C and GAPDH was used as a marker for the nuclear and cytoplasmic fraction, respectively. Red asterisks indicate increased interaction of mutant E418X, R635X with RelB without NIK expression. Blue asterisks indicate increased translocation of mutant forms E418X, R635X, and active form of NF-κB2 (p52) to the nucleus. Data shown are representative of 3 experiments.

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