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. 2004 Jul;24(13):5639–5649. doi: 10.1128/MCB.24.13.5639-5649.2004

FIG. 6.

FIG. 6.

Menin interacts with wild-type and oncogenic MLL proteins. (A and B) 293 cells were transiently transfected with expression vectors encoding various MLL deletion or fusion mutants (shown schematically in panel A) containing HIS and FLAG epitope tags at their N termini. Nuclear extracts prepared from transfectants were subjected to immunoprecipitation (IP) with anti-FLAG antibody (M2). Immune precipitates were analyzed by SDS-PAGE and were immunoblotted with antibodies indicated to the right of the respective panels (for panel B, anti-His [D-8] for various MLL mutants, anti-MLLC [mmC2.1], anti-HCF-1C [H12], and antimenin [C19], respectively). Positions of molecular size markers are indicated on the left. Coprecipitation of endogenous menin with exogenous MLL (+ or −) is indicated to the right of the schematic. (C) Nuclear extracts of REH and HB cells were subjected to immunoprecipitation using antimenin antibody (C19) or a negative control antibody (anti-DmMyb). Immune precipitates were analyzed by SDS-PAGE and were immunoblotted with anti-MLLN (mmN4.4, top gel), anti-MLLC (mmC2.1, middle gel), and anti-ENL antibodies (bottom gel) as indicated to the right of the panels. Wild-type MLL coprecipitated with menin in REH cells (lane 3). Both wild-type and fusion (MLL-ENL) MLL proteins coprecipitated with menin in HB cells (lane 6).