All TDP-43-bearing plasmids consisted of human TDP-43 fused at the C-terminus to EGFP (Fig. 1A). A linker region of 14 amino acids separates the C-terminus of TDP-43 from the N-terminus of EGFP, and six histidine residues were added to the C-terminus of EGFP to facilitate purification of the translated protein. The A315T mutation was created by site-directed mutagenesis of the adenine base at position 943 to guanine. The nuclear localization signal (NLS) was mutated by PCR as described (Winton et al., 2008 (link)) with the following primers: 5′– CAACTATCCAAAAGATAACGCAGCAGCAATGGATGAGACAGATGC–3′ and 5′– GCATCTGTCTCATCCATTGCTGCTGCGTTATCTTTTGGATAGTTG–3′. The nuclear export signal (NES) was disrupted similarly with the following primers: 5′–GCAGTCTCTTT GTGGAGAGGACGGAGGGGGAAAAGGAATCAGCGTTCATATATC–3′ and 5′– GATA TATGAACGCTGATTCCTTTTCCCCCTCCGTCCTCTCCACAAAGAGACTC –3′. Mutant huntingtin, mCherry, and EGFP were cloned into pGW1-CMV vectors as described (Arrasate et al., 2004 (link)). Sequence information for all plasmids is available at http://gind-db.ucsf.edu:8000/cgibin/Plasmid/main_menu2.cgi.