Fig. 4: Legionella infection causes ubiquitination of GRASP proteins, which is dependent on SidE effectors.
From: Serine-ubiquitination regulates Golgi morphology and the secretory pathway upon Legionella infection
A Ubiquitination assay of GRASP55-GFP purified from HEK293T cells infected with Legionella strains. HEK293T cells were seeded in 6-well plate and co-transfected with plasmids encoding C-terminally GFP tagged GRASP55 and FcγRII then were infected for indicated times with Legionella bacteria opsonized by Legionella antibody. Cells were lysed with IP lysis buffer and purified GRASP55 proteins were separated by SDS-PAGE followed by blotting using anti-GFP and anti-ubiquitin antibodies. B Ubiquitination assay of GRASP65-GFP purified from HEK293T cells infected by Legionella wild type or ΔdupA/B mutant. C Ubiquitination assay of GRASP55-GFP purified from HEK293T cells infected with Legionella wild-type, ΔsidEs or ΔdupA/B strains. D Ubiquitination assay of GRASP65-GFP purified from HEK293T cells infected with Legionella wild-type, ΔsidEs or ΔdupA/B strains.
