ArticleScientific reports2019
Unconventional secretion factor GRASP55 is increased by pharmacological unfolded protein response inducers in neurons.
Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed.
- PERK orchestrates an endoplasmic reticulum stress alternative splicing program via CLK1/SRSF1.Nature communications · 2026Article
- Endoplasmic reticulum and Golgi stress signaling-mediated regulation of protein secretion.Cellular & molecular biology letters · 2026Review
- Golgi Fragmentation as a Potential Link Between SARS-CoV-2 Infection and Alzheimer's Disease: Mechanisms and Implications for Neurodegeneration in Long COVID.Sub-cellular biochemistry · 2026Review
- GRASPs link Reelin to the Golgi during neocortical development to control neuronal migration and dendritogenesis.Communications biology · 2025Article
- Dendritic cell phagosomes recruit GRASP55 for export of antigen-loaded MHC molecules.Cell reports · 2025Article
- Article
- Review
- Neuron-specific translational control shift ensures proteostatic resilience during ER stress.The EMBO journal · 2022Article
- Unconventional Protein Secretion in Brain Tumors Biology: Enlightening the Mechanisms for Tumor Survival and Progression.Frontiers in cell and developmental biology · 2022Review
- PsGRASP, a Golgi Reassembly Stacking Protein inFrontiers in microbiology · 2021Article
- Nonredundant Roles of GRASP55 and GRASP65 in the Golgi Apparatus and Beyond.Trends in biochemical sciences · 2020Review
- Lyn kinase regulates egress of flaviviruses in autophagosome-derived organelles.Nature communications · 2020Article
- The function of GORASPs in Golgi apparatus organization in vivo.The Journal of cell biology · 2020Article
- The UPR in Neurodegenerative Disease: Not Just an Inside Job.Biomolecules · 2020Review
- Nucleation-dependent amyloid fibrillation of human GRASP55 in aqueous solution.European biophysics journal : EBJ · 2020Article
- No evidence for cell-to-cell transmission of the unfolded protein response in cell culture.Journal of neurochemistry · 2020Article
- New Insights Into the Golgi Stacking Proteins.Frontiers in cell and developmental biology · 2019Review
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Authors and funding
5 authors.
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Abstract
Accumulation of misfolded proteins in the endoplasmic reticulum (ER), defined as ER stress, results in activation of the unfolded protein response (UPR). UPR activation is commonly observed in neurodegenerative diseases. ER stress can trigger unconventional secretion mediated by Golgi reassembly and stacking proteins (GRASP) relocalization in cell lines. Here we study the regulation of GRASP55 by the UPR upon pharmacological induction of ER stress in primary mouse neurons. We demonstrate that UPR activation induces mRNA and protein expression of GRASP55, but not GRASP65, in cortical neurons. UPR activation does not result in relocalization of GRASP55. UPR-induced GRASP55 expression is reduced by inhibition of the PERK pathway of the UPR and abolished by inhibition of the endonuclease activity of the UPR transducer IRE1. Expression of the IRE1 target XBP1s in the absence of ER stress is not sufficient to increase GRASP55 expression. Knockdown of GRASP55 affects neither induction nor recovery of the UPR. We conclude that the UPR regulates the unconventional secretion factor GRASP55 via a mechanism that requires the IRE1 and the PERK pathway of the UPR in neurons.
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