Supplementary Figure 3: cGAS interacts with CCP5 and CCP6 but not with other members of the CCP family. | Nature Immunology

Supplementary Figure 3: cGAS interacts with CCP5 and CCP6 but not with other members of the CCP family.

From: Glutamylation of the DNA sensor cGAS regulates its binding and synthase activity in antiviral immunity

Supplementary Figure 3

(a) cGAS peptide sequences identified by mass spectrometry. (b) GST-tagged WT (FL) or catalytic domain truncated (Δ160–424) CCP5 were incubated with BMDM lysates for 4 h, followed by a GST pulldown assay. Precipitates were immunoblotted with the indicated antibodies. (c) WT BMDMs were stained with antibodies against β-tubulin, cGAS and CCP6, followed by confocal microscopy. Scale bar, 10 μm. (d) WT BMDMs treated with 10 μM CoCl2 or 2 μM phenanthroline for 6 h were immunoprecipitated with antibody against CCP6, followed by immunoblotting with the indicated antibodies. (e) GST-tagged WT (FL) or catalytic domain truncated (Δ230–401) CCP6 were incubated with BMDM lysates for 4 h, followed by a GST pulldown assay. Precipitates were immunoblotted with the indicated antibodies. (f) Schematic representation of putative glutamylation sites on cGAS. (g, h) Structural illustration of two putative glutamylation sites on cGAS (PDB code 4K97). Putative glutamylation sites were marked in red and the catalytic residues were marked in purple. Data are representative of at least three independent experiments.

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