2010/08/01 by Oliver Kepp, Abdelaziz Gdoura, Isabelle Martins +12 · 1 citation
Immunology and Microbiology · Biochemistry, Genetics and Molecular Biology · #Phagocytosis and Immune Regulation #Immune Cell Function and Interaction #Endoplasmic Reticulum Stress and Disease
paper · doi:10.4161/cc.9.15.12459
openalex publication_date 2010/08/01 · openalex created_date 2025/10/10 · openalex updated_date 2026/07/29
In response to immunogenic cell death inducers, calreticulin (CRT) translocates from its orthotopic localization in the lumen of the endoplasmic reticulum (ER) to the surface of the plasma membrane where it serves as an engulfment signal for antigen-presenting cells.(1) Here, we report that yet another ER protein, the lysyl-tRNA synthetase (KARS), was exposed on the surface of stressed cells, on which KARS co-localized with CRT in lipid rafts. Depletion of KARS with small interfering RNAs suppressed CRT exposure induced by anthracyclines or UVC light. In contrast to CRT, KARS was also found in the supernatant of stressed cells. Recombinant KARS protein was unable to influence the binding of recombinant CRT to the cell surface. Moreover, recombinant KARS protein was unable to stimulate macrophages in vitro. These results underscore the contribution of KARS to the emission of (one of) the principal signal(s) of immunogenic cell death, CRT exposure.