Subcellular localization of full-length human myeloid leukemia factor 1 (MLF1) is independent of 14-3-3 proteins

Cellular & Molecular Biology Letters

Manuela Molzan¹  Christian Ottmann² 

[1] Chemical Genomics Centre of the Max-Planck-Society, Dortmund, Germany$$;Chemical Genomics Centre of the Max-Planck-Society, Dortmund, Germany$$Laboratory of Chemical Biology, Department of Biomedical Engineering, Technische Universiteit Eindhoven, Eindhoven, The Netherlands$$

关键词: MLF1;    14-3-3;    Binding site;    Protein-protein interactions;    Subcellular localization;    Acute myeloid leukemia;    Myelodysplastic syndrome;    Site-directed mutagenesis;    Confocal microscopy;    Live cell imaging;   

DOI  :  10.2478/s11658-012-0044-1

学科分类：分子生物学，细胞生物学和基因

来源: Uniwersytet Wroclawski * Wydzial Biotechnologii / University of Wroclaw, Faculty of Biotechnology

【 摘 要 】

Myeloid leukemia factor 1 (MLF1) is associated with the development of leukemic diseases such as acute myeloid leukemia (AML) and myelodysplastic syndrome (MDS). However, information on the physiological function of MLF1 is limited and mostly derived from studies identifying MLF1 interaction partners like CSN3, MLF1IP, MADM, Manp and the 14-3-3 proteins. The 14-3-3-binding site surrounding S34 is one of the only known functional features of the MLF1 sequence, along with one nuclear export sequence (NES) and two nuclear localization sequences (NLS). It was recently shown that the subcellular localization of mouse MLF1 is dependent on 14-3-3 proteins. Based on these findings, we investigated whether the subcellular localization of human MLF1 was also directly 14-3-3-dependent. Live cell imaging with GFP-fused human MLF1 was used to study the effects of mutations and deletions on its subcellular localization. Surprisingly, we found that the subcellular localization of full-length human MLF1 is 14-3-3-independent, and is probably regulated by other as-yet-unknown proteins.

【 授权许可】

Unknown