Lysyl tRNA synthetase is required for the translocation of calreticulin to the cell surface in immunogenic death

Abstract

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.


Autore Pugliese

Tutti gli autori

  • Kepp O. , Gdoura A. , Martins I. , Panaretakis T. , Schlemmer F. , Tesniere A. , Fimia G.M. , Ciccosanti F. , Burgevin A. , Piacentini M. , Eggleton P. , Young P.J. , Zitvogel L. , van Endert P. , Kroemer G.

Titolo volume/Rivista

CELL CYCLE


Anno di pubblicazione

2010

ISSN

1551-4005

ISBN

Non Disponibile


Numero di citazioni Wos

14

Ultimo Aggiornamento Citazioni

25/04/2018


Numero di citazioni Scopus

15

Ultimo Aggiornamento Citazioni

26/04/2018


Settori ERC

Non Disponibile

Codici ASJC

Non Disponibile