Endoplasmic reticulum stress reduces the export from the ER and alters the architecture of post-ER compartments

Giuseppina Amodio, Maurizio Renna, Simona Paladino, Consuelo Venturi, Carlo Tacchetti, Ornella Moltedo, Silvia Franceschelli, Massimo Mallardo, Stefano Bonatti, Paolo Remondelli

Research output: Contribution to journalArticlepeer-review


In eukaryotic cells several physiologic and pathologic conditions generate the accumulation of unfolded proteins in the endoplasmic reticulum (ER), leading to ER stress. To restore normal function, some ER transmembrane proteins sense the ER stress and activate coordinated signalling pathways collectively called the Unfolded Protein Response (UPR). Little is known on how the UPR relates to post-ER compartments and to the export from the ER of newly synthesized proteins. Here, we report that the ER stress response induced by either thapsigargin or nitric oxide modifies the dynamics of the intracellular distribution of ERGIC-53 and GM130, two markers of the ER Golgi Intermediate Compartment and of the cis-Golgi, respectively. In addition, induction of ER stress alters the morphology of the ERGIC and the Golgi complex and interferes with the reformation of both compartments. Moreover, ER stress rapidly reduces the transport to the Golgi complex of the temperature sensitive mutant of the Vesicular Stomatitis Virus G Glycoprotein (VSV-G) fused with the Green Fluorescent Protein (ts045G), without apparently decreasing the amount of the protein competent for export. Interestingly, a parallel rapid reduction of the number of Sec31 labelled fluorescent puncta on the ER membranes does occur, thus suggesting that the ER stress alters the ER export and the dynamic of post-ER compartments by rapidly targeting the formation of COPII-coated transport intermediates.

Original languageEnglish
Pages (from-to)2511-2521
Number of pages11
JournalInternational Journal of Biochemistry and Cell Biology
Issue number12
Publication statusPublished - Dec 2009


  • Endoplasmic reticulum stress
  • ERGIC-53
  • GM130
  • Unfolded Protein Response
  • VSV-G

ASJC Scopus subject areas

  • Biochemistry
  • Cell Biology


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