The hydrophobic residues within the C-terminal domain of GNL3L constitute a functional nuclear export signal.

<p>(<b>A</b>) Indicated variants of GNL3L ^51–582-GFP and GNL3L ^501–582-GFP were generated using QuickChange site-directed mutagenesis as described in Materials and Methods. (<b>B</b>) All the indicated GNL3L mutants were expressed correct size polypeptides as evident from the western blot analysis using anti-GFP antibody. HeLa cells were transfected with wild type GNL3L ^51–582-GFP or GNL3L ^501–582-GFP (<b>C</b>) and their variants (<b>D</b>). Transfected cells were fixed in 3% paraformaldehyde and nuclei were stained using DAPI. Subcellular localization GNL3L variants were analyzed using confocal microscope. The scale bar represents 20 μm.