Klin Padiatr 2020; 232(03): e1
DOI: 10.1055/s-0040-1709761
Abstracts

Small changes in the MLL-AF4 fusion protein make a difference

Authors

  • A Siemund

    1   Institute of Pharmaceutical Biology/DCAL, Goethe-University of Frankfurt, Biocenter, Max-von-Laue-Str. 9, D-60438 Frankfurt/Main, Germany

  • E Kowarz

    1   Institute of Pharmaceutical Biology/DCAL, Goethe-University of Frankfurt, Biocenter, Max-von-Laue-Str. 9, D-60438 Frankfurt/Main, Germany

  • R Marschalek

    1   Institute of Pharmaceutical Biology/DCAL, Goethe-University of Frankfurt, Biocenter, Max-von-Laue-Str. 9, D-60438 Frankfurt/Main, Germany
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We have studied the human MLL-AF4 fusion protein and compared it functionally with a murinized version, where have exchanged only the pSER domain (~120 amino acids) with murine Af4 sequences (MLL-murAF4). We have studied these MLL fusion proteins alone and in combination with the reciprocal AF4-MLL fusion proteins in a stably transfected cell line model. To our surprise, The MLL-murAF4 fusion displayed partial gain-of-funcions as well as a loss-of-function phenoytpe, e.g. by loosing its ability to show any synergism with the reciprocal AF4-MLL fusion protein at target genes. Moreover, we have investigated the target gene profile by the massive amplification of cDNA ends (MACE) technology. All findings will be discussed.


Publication History

Article published online:
13 May 2020

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