ArticleMolecular biology of the cell2005
dGRASP localization and function in the early exocytic pathway in Drosophila S2 cells.
Article in Molecular biology of the cell, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.
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Who cites it
51 citing papers in PubMed, 94 citations in OpenAlex.
- Unconventional Protein Transport Across the Golgi Ribbon.Sub-cellular biochemistry · 2026Review
- Article
- Golgi defect as a major contributor to lysosomal dysfunction.Frontiers in cell and developmental biology · 2024Review
- Article
- A distinct Golgi-targeting mechanism of dGM130 inFrontiers in molecular neuroscience · 2023Article
- Rapid degradation of GRASP55 and GRASP65 reveals their immediate impact on the Golgi structure.The Journal of cell biology · 2021Article
- Nonredundant Roles of GRASP55 and GRASP65 in the Golgi Apparatus and Beyond.Trends in biochemical sciences · 2020Review
- The function of GORASPs in Golgi apparatus organization in vivo.The Journal of cell biology · 2020Article
- Article
- Tales of the ER-Golgi Frontier:Frontiers in cell and developmental biology · 2020Review
- Golgin45-Syntaxin5 Interaction Contributes to Structural Integrity of the Golgi Stack.Scientific reports · 2019Article
- A New Look at the Functional Organization of the Golgi Ribbon.Frontiers in cell and developmental biology · 2019Article
- The yeast GRASP Grh1 displays a high polypeptide backbone mobility along with an amyloidogenic behavior.Scientific reports · 2018Article
- Structural Basis for the Interaction between Golgi Reassembly-stacking Protein GRASP55 and Golgin45.The Journal of biological chemistry · 2017Article
- Glycosylation Quality Control by the Golgi Structure.Journal of molecular biology · 2016Review
- GRASP: A Multitasking Tether.Frontiers in cell and developmental biology · 2016Review
- Loss of a Clueless-dGRASP complex results in ER stress and blocks Integrin exit from the perinuclear endoplasmic reticulum in Drosophila larval muscle.Biology open · 2015Article
- GRASPs in Golgi Structure and Function.Frontiers in cell and developmental biology · 2015Review
- GRASP65 controls the cis Golgi integrity in vivo.Biology open · 2014Article
- Membrane adhesion dictates Golgi stacking and cisternal morphology.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The de novo model for Golgi stack biogenesis predicts that membrane exiting the ER at transitional ER (tER) sites contains and recruits all the necessary molecules to form a Golgi stack, including the Golgi matrix proteins, p115, GM130, and GRASP65/55. These proteins leave the tER sites faster than Golgi transmembrane resident enzymes, suggesting that they act as a template nucleating the formation of the Golgi apparatus. However, the localization of the Golgi matrix proteins at tER sites is only shown under conditions where exit from the ER is blocked. Here, we show in Drosophila S2 cells, that dGRASP, the single Drosophila homologue of GRASP65/55, localizes both to the Golgi membranes and the tER sites at steady state and that the myristoylation of glycine 2 is essential for the localization to both compartments. Its depletion for 96 h by RNAi gave an effect on the architecture of the Golgi stacks in 30% of the cells, but a double depletion of dGRASP and dGM130 led to the quantitative conversion of Golgi stacks into clusters of vesicles and tubules, often featuring single cisternae. This disruption of Golgi architecture was not accompanied by the disorganization of tER sites or the inhibition of anterograde transport. This shows that, at least in Drosophila, the structural integrity of the Golgi stacks is not required for efficient transport. Overall, dGRASP exhibits a dynamic association to the membrane of the early exocytic pathway and is involved in Golgi stack architecture.
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