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The TRAPP complex mediates secretion arrest induced by stress granule assembly
Author(s) -
Zappa Francesca,
Wilson Cathal,
Di Tullio Giuseppe,
Santoro Michele,
Pucci Piero,
Monti Maria,
D'Amico Davide,
PisoneroVaquero Sandra,
De Cegli Rossella,
Romano Alessia,
Saleem Moin A,
Polishchuk Elena,
Failli Mario,
Giaquinto Laura,
De Matteis Maria Antonietta
Publication year - 2019
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.15252/embj.2019101704
Subject(s) - biology , secretion , stress granule , microbiology and biotechnology , granule (geology) , biochemistry , gene , paleontology , translation (biology) , messenger rna
The TRA nsport 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 ( SG s) leading to vesiculation of the Golgi complex and arrest of ER export. The relocation of the TRAPP complex and COPII to SG s only occurs in cycling cells and is CDK 1/2‐dependent, being driven by the interaction of TRAPP with hn RNPK , a CDK substrate that associates with SG s when phosphorylated. In addition, CDK 1/2 inhibition impairs TRAPP complex/ COPII relocation to SG s while stabilizing them at ER exit sites. Importantly, the TRAPP complex controls the maturation of SG s. SG s that assemble in TRAPP ‐depleted cells are smaller and are no longer able to recruit RACK 1 and Raptor, two TRAPP ‐interactive signaling proteins, sensitizing cells to stress‐induced apoptosis.