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The TRAPP complex mediates secretion arrest induced by stress granule assembly

Research output: Contribution to journalArticle

  • Francesca Zappa
  • Cathal Wilson
  • Giuseppe Di Tullio
  • Michele Santoro
  • Piero Pucci
  • Maria Monti
  • Davide D'Amico
  • Sandra Pisonero-Vaquero
  • Rossella De Cegli
  • Alessia Romano
  • Moin A Saleem
  • Elena Polishchuk
  • Mario Failli
  • Laura Giaquinto
  • Maria Antonietta De Matteis
Original languageEnglish
Article numbere101704
Number of pages24
JournalEMBO Journal
Issue number19
Early online date20 Aug 2019
DateAccepted/In press - 1 Aug 2019
DateE-pub ahead of print - 20 Aug 2019
DatePublished (current) - 1 Oct 2019


The TRAnsport Protein Particle (TRAPP) complex controls multiple membrane trafficking steps and is strategically positioned to mediate cell adaptation to diverse environmental conditions, including acute stress. We have identified the TRAPP complex as a component of a branch of the integrated stress response that impinges on the early secretory pathway. The TRAPP complex associates with and drives the recruitment of the COPII coat to stress granules (SGs) leading to vesiculation of the Golgi complex and arrest of ER export. The relocation of the TRAPP complex and COPII to SGs only occurs in cycling cells and is CDK1/2‐dependent, being driven by the interaction of TRAPP with hnRNPK, a CDK substrate that associates with SGs when phosphorylated. In addition, CDK1/2 inhibition impairs TRAPP complex/COPII relocation to SGs while stabilizing them at ER exit sites. Importantly, the TRAPP complex controls the maturation of SGs. SGs that assemble in TRAPP‐depleted cells are smaller and are no longer able to recruit RACK1 and Raptor, two TRAPP‐interactive signaling proteins, sensitizing cells to stress‐induced apoptosis.

    Research areas

  • Cdk, COPII, integrated stress response, stress granules, TRAPP complex



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    Embargo ends: 20/02/20

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