Skip to main content
. 2009 Apr 21;106(18):7607–7612. doi: 10.1073/pnas.0900688106

Fig. 2.

Fig. 2.

The 25-kDa C-terminal fragment of TDP-43 is prone to phosphorylation, but its phosphorylation is not required for inclusion formation. (A) Cells were transfected for GFP-TDP-43 or GFP-TDP-25, then immunostained with anti-pTDP-43, which detects TDP-43 when phosphorylated at S409/S410. Fluorescent confocal microscopy demonstrates enhanced staining of GFP-TDP-25 compared with GFP-TDP-43. (B) Lysates from HEK293 cells transfected with GFP-TDP-43, GFP-TDP-43NLSmut, GFP-TDP-25, or GFP-TDP-25S409A/S410A were subjected to Western blot analysis and probed with anti-pTDP-43. The 25-kDa C-terminal fragment showed marked anti-pTDP-43 immunoreactivity compared with GFP-TDP-43 or GFP-TDP-43NLSmut. GFP-TDP-25S409A/S410A did not exhibit any immunoreactivity. The membrane was reprobed with anti-GAPDH to verify protein loading. (C) Fluorescent confocal microscopy demonstrates that GFP-TDP-25S409A/S410A, which is not phosphorylated at S409/S410, can form cytoplasmic inclusions.