Thiol-mediated protein retention in the endoplasmic reticulum: The role of ERp44

Tiziana Anelli, Massimo Alessio, Angela Bachi, Leda Bergamelli, Gloria Bertoli, Serena Camerini, Alexandre Mezghrani, Elena Ruffato, Thomas Simmen, Roberto Sitia

Research output: Contribution to journalArticle

Abstract

Formation of disulfide bonds, an essential step for the maturation and exit of secretory proteins from the endoplasmic reticulum (ER), is controlled by specific ER-resident enzymes. A pivotal element in this process is Ero1α, an oxidoreductin that lacks known ER retention motifs. Here we show that ERp44 mediates Ero1α ER localization through the formation of reversible mixed disulfides. ERp44 also prevents the secretion of an unassembled cargo protein with unpaired cysteines. We conclude that ERp44 is a key element in thiol-mediated retention. It might also favour the maturation of disulfide-linked oligomeric proteins and their quality control.

Original languageEnglish
Pages (from-to)5015-5022
Number of pages8
JournalEMBO Journal
Volume22
Issue number19
DOIs
Publication statusPublished - Oct 1 2003

Keywords

  • Disulfide bond formation
  • IgM polymerization
  • Protein secretion
  • Quality control
  • Redox regulation

ASJC Scopus subject areas

  • Genetics
  • Cell Biology

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    Anelli, T., Alessio, M., Bachi, A., Bergamelli, L., Bertoli, G., Camerini, S., Mezghrani, A., Ruffato, E., Simmen, T., & Sitia, R. (2003). Thiol-mediated protein retention in the endoplasmic reticulum: The role of ERp44. EMBO Journal, 22(19), 5015-5022. https://doi.org/10.1093/emboj/cdg491