Identification of Novel Nuclear Localization Signals of Drosophila Myeloid Leukemia Factor

Citations Over Time

Abstract

Myeloid leukemia factor 1 (MLF1) was first identified as part of a leukemic fusion protein produced by a chromosomal translocation, and MLF family proteins are present in many animals. In mammalian cells, MLF1 has been described as mainly cytoplasmic, but in Drosophila, one of the dMLF isoforms (dMLFA) localized mainly in the nucleus while the other isoform (dMLFB), that appears to be produced by the alternative splicing, displays both nuclear and cytoplasmic localization. To investigate the difference in subcellular localization between MLF family members, we examined the subcellular localization of deletion mutants of dMLFA isoform. The analyses showed that the C-terminal 40 amino acid region of dMLFA is necessary and sufficient for nuclear localization. Based on amino acid sequences, we hypothesized that two nuclear localization signals (NLSs) are present within the region. Site-directed mutagenesis of critical residues within the two putative NLSs leads to loss of nuclear localization, suggesting that both NLS motifs are necessary for nuclear localization.

Related Papers

• → Identification of nuclear localization signal and nuclear export signal of VP1 from the chicken anemia virus and effects on VP2 shuttling in cells(2019)24 cited
• → Nuclear localization of Tob is important for regulation of its antiproliferative activity(2004)58 cited
• → Nucleo-cytoplasmic shuttling of human Kank protein accompanies intracellular translocation of β-catenin(2006)34 cited
• → Regulation of subcellular localization of the antiproliferative protein Tob by its nuclear export signal and bipartite nuclear localization signal sequences(2004)22 cited
• → Control of the nuclear localization of Extradenticle by competing nuclear import and export signals(1999)236 cited