Cytoplasmic HMGB2 orchestrates CALR translocation in the course of immunogenic cell death

Oncoimmunology. 2024 Dec 31;13(1):2421028. doi: 10.1080/2162402X.2024.2421028. Epub 2024 Oct 26.

Abstract

A recent in vitro study showed that pharmacological inhibition of the nuclear export receptor XPO1 suppresses oxaliplatin-induced nuclear release of HMGB1 and HMGB2, as well as the translocation of CALR to the plasma membrane. Moreover, cell-targeted-HMGB2 protein potently induced CALR exposure, even in the absence of oxaliplatin.

Keywords: Adjuvanticity; Calreticulin; Immunotherapy; checkpoint blockade.

MeSH terms

  • Animals
  • Antineoplastic Agents / pharmacology
  • Calreticulin* / metabolism
  • Cytoplasm / metabolism
  • Exportin 1 Protein
  • HMGB1 Protein / metabolism
  • HMGB2 Protein* / genetics
  • HMGB2 Protein* / metabolism
  • Humans
  • Immunogenic Cell Death* / drug effects
  • Karyopherins / metabolism
  • Oxaliplatin / pharmacology
  • Protein Transport
  • Receptors, Cytoplasmic and Nuclear / metabolism

Substances

  • Calreticulin
  • HMGB2 Protein
  • HMGB1 Protein
  • CALR protein, human
  • Karyopherins
  • Antineoplastic Agents
  • Oxaliplatin
  • Exportin 1 Protein
  • Receptors, Cytoplasmic and Nuclear