ArticleMolecular biology of the cell2008
The role of GRASP55 in Golgi fragmentation and entry of cells into mitosis.
Article in Molecular biology of the cell, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.
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Who cites it
53 citing papers in PubMed.
- Protein Kinase D2 Regulates GRASP65 Phosphorylation and Golgi Ribbon Unlinking During G2/M Transition.Cells · 2026Article
- The Impact of Golgi Organization on Cell Cycle and Cancer Development.Sub-cellular biochemistry · 2026Review
- Dendritic cell phagosomes recruit GRASP55 for export of antigen-loaded MHC molecules.Cell reports · 2025Article
- RNA scaffolds the Golgi ribbon by forming condensates with GM130.Nature cell biology · 2024Article
- Article
- FvKex2 is required for development, virulence, and mycotoxin production in Fusarium verticillioides.Applied microbiology and biotechnology · 2024Article
- The crescent-like Golgi ribbon is shaped by the Ajuba/PRMT5/Aurora-A complex-modified HURP.Cell communication and signaling : CCS · 2023Article
- Impact of interorganelle coordination between the conventional early secretory pathway and autophagy in cellular homeostasis and stress response.Frontiers in cell and developmental biology · 2023Review
- GRASP55 restricts early-stage autophagy and regulates spatial organization of the early secretory network.Biology open · 2021Article
- Gβγ regulates mitotic Golgi fragmentation and G2/M cell cycle progression.Molecular biology of the cell · 2021Article
- 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
- SIRT2 deacetylates GRASP55 to facilitate post-mitotic Golgi assembly.Journal of cell science · 2019Article
- GORASP2/GRASP55 collaborates with the PtdIns3K UVRAG complex to facilitate autophagosome-lysosome fusion.Autophagy · 2019Article
- GRASP depletion-mediated Golgi destruction decreases cell adhesion and migration via the reduction of α5β1 integrin.Molecular biology of the cell · 2019Article
- DjA1 maintains Golgi integrity via interaction with GRASP65.Molecular biology of the cell · 2019Article
- A New Look at the Functional Organization of the Golgi Ribbon.Frontiers in cell and developmental biology · 2019Article
- Golgi Structure and Function in Health, Stress, and Diseases.Results and problems in cell differentiation · 2019Review
- Golgi ribbon disassembly during mitosis, differentiation and disease progression.Current opinion in cell biology · 2017Review
Corrections and comments
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Authors and funding
9 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
GRASP55 is a Golgi-associated protein, but its function at the Golgi remains unclear. Addition of full-length GRASP55, GRASP55-specific peptides, or an anti-GRASP55 antibody inhibited Golgi fragmentation by mitotic extracts in vitro, and entry of cells into mitosis. Phospho-peptide mapping of full-length GRASP55 revealed that threonine 225 and 249 were mitotically phosphorylated. Wild-type peptides containing T225 and T249 inhibited Golgi fragmentation and entry of cells into mitosis. Mutant peptides containing T225E and T249E, in contrast, did not affect Golgi fragmentation and entry into mitosis. These findings reveal a role of GRASP55 in events leading to Golgi fragmentation and the subsequent entry of cell into mitosis. Surprisingly, however, under our experimental conditions, >85% knockdown of GRASP55 did not affect the overall organization of Golgi organization in terms of cisternal stacking and lateral connections between stacks. Based on our findings we suggest that phosphorylation of GRASP55 at T225/T249 releases a bound component, which is phosphorylated and necessary for Golgi fragmentation. Thus, GRASP55 has no role in the organization of Golgi membranes per se, but it controls their fragmentation by regulating the release of a partner, which requires a G2-specific phosphorylation at T225/T249.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.