Unconventional secretion: a stress on GRASP

Fabrizio Giuliani, Adam Grieve, Catherine Rabouille

Research output: Contribution to journalReview article (Academic Journal)peer-review

97 Citations (Scopus)


Most proteins follow the classical secretory pathway from the endoplasmic reticulum, via the Golgi, to the plasma membrane or extracellular medium. However, some proteins reach these final destinations by two alternative routes. One sustains the extracellular delivery of cytoplasmic proteins that lack a signal peptide, the other supports the transport of transmembrane proteins to the plasma membrane in a manner that bypasses the Golgi. Here, we highlight the observation that some unconventional secretion events are triggered by cellular stress. Furthermore, one Golgi protein, Golgi Re-Assembly and Stacking Protein (GRASP), has been shown to be essential to both types of unconventional secretion and we discuss ways in which it may support these events in a Golgi-independent manner.

Original languageEnglish
Pages (from-to)498-504
Number of pages7
JournalCurrent Opinion in Cell Biology
Issue number4
Publication statusPublished - Aug 2011

Bibliographical note

Copyright © 2011 Elsevier Ltd. All rights reserved.


  • Animals
  • Cell Membrane/metabolism
  • Endoplasmic Reticulum/metabolism
  • Golgi Apparatus/metabolism
  • Humans
  • Membrane Proteins/metabolism
  • Secretory Pathway
  • Yeasts/cytology


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