Fig. 2: TASL-SLC15A4 interaction is necessary for endolysosomal TLR signaling.
From: Structural basis for recruitment of TASL by SLC15A4 in human endolysosomal TLR signaling
a, b Confocal microscopy images of HEK293T cells co-transfected with SLC15A4-mCherry and TASL(1–20)-EGFP (WT or mutations) plasmids (a) or TASL(1–20)-EGFP and SLC15A4-mCherry (WT or mutations) plasmids (b). Localization of SLC15A4 and TASL are shown. Data are representative of three biological independent experiments. S154-mCherry, SLC15A4-mCherry. Scale bars, 5 μm. c, d Mutations of interface residues in either TASL (c) or SLC15A4 (d) abolished or diminished the TASL-SLC15A4 interaction. Data are representative of two biological independent experiments. S154, SLC15A4. WCE, whole-cell extract. e, f Mutations of interface residues in both TASL (e) and SLC15A4 (f) abolished or diminished the R848-stimulated IL-8 expression in THP1 cells. THP1 TASL-null cells were reconstituted with TASL wild type or mutants (e), whereas THP1 SLC15A4-null cells were reconstituted with SLC15A4 wild type or mutants (f). Graphs show mean ± s.d. of stimulation replicates (n = 3 biological replicates) from one experiment representative of two independent experiments. S154, SLC15A4. Source data for relevant information are provided as a Source Data file.
