Figure 4. The function of LGP2 in sensing unedited self RNA involves its canonical role as dsRNA sensor that requires RNA binding and ATP hydrolysis.

1. Schematic illustration of the domain structure of LGP2 and various point mutants and truncation mutants that are used in this study. The N‐terminal domain (NTD) of LGP2 is composed of a conserved DExH/D helicase domain, subdivided into the helicase 1 (Hel1), helicase 2 (Hel2) and helicase insertion (Hel2i) domain, and a pincer motif (P). The NTD is followed by a C‐terminal domain (CTD), involved in RNA binding.
2. HEK293 WT or ADAR1‐knockout cells (clone 1) were transiently transfected with an empty vector (EV) or a vector encoding the indicated WT, truncation, or point mutant(s) of LGP2. Cells were harvested 72 h post‐transfection and the type I IFN response was monitored by RT‐qPCR analysis of IFN‐β and IFIT1 transcript expression, normalized to ACTB. Data are means ± s.d. from a representative of three biological replicate experiments.
3. Cells were treated as in (B). Protein lysates were prepared and analyzed by SDS‐PAGE followed by immunoblotting using the indicated antibodies (n = 3). The dotted line indicates the juxtaposition of two nonadjacent lanes.

Source data are available online for this figure.