ArticleThe Journal of biological chemistry2013
Structural insight into Golgi membrane stacking by GRASP65 and GRASP55 proteins.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed.
- Collective behavior of "flexicles".Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- The crescent-like Golgi ribbon is shaped by the Ajuba/PRMT5/Aurora-A complex-modified HURP.Cell communication and signaling : CCS · 2023Article
- Biogenesis of JC polyomavirus associated extracellular vesicles.Journal of extracellular biology · 2022Article
- Rapid degradation of GRASP55 and GRASP65 reveals their immediate impact on the Golgi structure.The Journal of cell biology · 2021Article
- Visualizing insulin vesicle neighborhoods in β cells by cryo-electron tomography.Science advances · 2020Article
- Nonredundant Roles of GRASP55 and GRASP65 in the Golgi Apparatus and Beyond.Trends in biochemical sciences · 2020Review
- 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
- Self-Association of Purified Reconstituted ER Luminal Spacer Climp63.Frontiers in cell and developmental biology · 2020Article
- Article
- DjA1 maintains Golgi integrity via interaction with GRASP65.Molecular biology of the cell · 2019Article
- Unconventional secretion factor GRASP55 is increased by pharmacological unfolded protein response inducers in neurons.Scientific reports · 2019Article
- The yeast GRASP Grh1 displays a high polypeptide backbone mobility along with an amyloidogenic behavior.Scientific reports · 2018Article
- Knockout of the Golgi stacking proteins GRASP55 and GRASP65 impairs Golgi structure and function.Molecular biology of the cell · 2017Article
- Going deep into protein secondary structure with synchrotron radiation circular dichroism spectroscopy.Biophysical reviews · 2017Review
- Structural Basis for the Interaction between Golgi Reassembly-stacking Protein GRASP55 and Golgin45.The Journal of biological chemistry · 2017Article
- Golgi structure formation, function, and post-translational modifications in mammalian cells.F1000Research · 2017Review
- Glycosylation Quality Control by the Golgi Structure.Journal of molecular biology · 2016Review
- New structural insights into Golgi Reassembly and Stacking Protein (GRASP) in solution.Scientific reports · 2016Article
- GRASP: A Multitasking Tether.Frontiers in cell and developmental biology · 2016Review
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Authors and funding
7 authors.
Funding
Abstract
The stacking of Golgi cisternae involves GRASP65 and GRASP55. The oligomerization of the N-terminal GRASP domain of these proteins, which consists of two tandem PDZ domains, is required to tether the Golgi membranes. However, the molecular basis for GRASP assembly is unclear. Here, we determined the crystal structures of the GRASP domain of GRASP65 and GRASP55. The structures reveal similar homotypic interactions: the GRASP domain forms a dimer in which the peptide-binding pockets of the two neighboring PDZ2 domains face each other, and the dimers are further connected by the C-terminal tail of one GRASP domain inserting into the binding pocket of the PDZ1 domain in another dimer. Biochemical analysis suggests that both types of contacts are relatively weak but are needed in combination for GRASP-mediated Golgi stacking. Our results unveil a novel mode of membrane tethering by GRASP proteins and provide insight into the mechanism of Golgi stacking.
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