ArticleThe Journal of cell biology2007
The yeast orthologue of GRASP65 forms a complex with a coiled-coil protein that contributes to ER to Golgi traffic.
Article in The Journal of cell biology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 77 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
77 citing papers in PubMed, 156 citations in OpenAlex.
- The role of N-terminal acetylation on biomolecular condensation.Communications chemistry · 2026Article
- N-terminal acetylation controls multiple functional aspects of the influenza A virus ribonuclease PA-X.Journal of virology · 2026Article
- Plant Golgi and GECCO: The Universality of ER-Golgi Interface.Sub-cellular biochemistry · 2026Review
- NAA60 facilitates LRRC8A- and LRRC8D-mediated platinum drug uptake.Communications biology · 2025Article
- N-terminal acetylation controls multiple functional aspects of the influenza A virus ribonuclease PA-X.bioRxiv : the preprint server for biology · 2025Article
- The Plasmodium GRASP Homolog Modulates Liver Stage Development, Subsequent Blood Infection and Virulence in Mice.Molecular microbiology · 2025Article
- Dendritic cell phagosomes recruit GRASP55 for export of antigen-loaded MHC molecules.Cell reports · 2025Article
- The potential role of liquid-liquid phase separation in the cellular fate of the compartments for unconventional protein secretion.Protein science : a publication of the Protein Society · 2024Article
- Spatiotemporal dissection of the Golgi apparatus and the ER-Golgi intermediate compartment in budding yeast.eLife · 2024Article
- Article
- Yeast Svf1 binds ceramides and contributes to sphingolipid metabolism at the ER cis-Golgi interface.The Journal of cell biology · 2023Article
- NAA60 (HAT4): the newly discovered bi-functional Golgi member of the acetyltransferase family.Clinical epigenetics · 2022Review
- From Nucleus to Membrane: A Subcellular Map of the N-Acetylation Machinery in Plants.International journal of molecular sciences · 2022Review
- Pathway engineering facilitates efficient protein expression in Pichia pastoris.Applied microbiology and biotechnology · 2022Review
- Computed structures of core eukaryotic protein complexes.Science (New York, N.Y.) · 2021Article
- GRASP55 restricts early-stage autophagy and regulates spatial organization of the early secretory network.Biology open · 2021Article
- An mTORC1-GRASP55 signaling axis controls unconventional secretion to reshape the extracellular proteome upon stress.Molecular cell · 2021Article
- Article
- Human NAA30 can rescue yeast mak3∆ mutant growth phenotypes.Bioscience reports · 2021Article
- PsGRASP, a Golgi Reassembly Stacking Protein inFrontiers in microbiology · 2021Article
17 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 3 institutions in 3 countries.
Funding
Abstract
The mammalian Golgi protein GRASP65 is required in assays that reconstitute cisternal stacking and vesicle tethering. Attached to membranes by an N-terminal myristoyl group, it recruits the coiled-coil protein GM130. The relevance of this system to budding yeasts has been unclear, as they lack an obvious orthologue of GM130, and their only GRASP65 relative (Grh1) lacks a myristoylation site and has even been suggested to act in a mitotic checkpoint. In this study, we show that Grh1 has an N-terminal amphipathic helix that is N-terminally acetylated and mediates association with the cis-Golgi. We find that Grh1 forms a complex with a previously uncharacterized coiled-coil protein, Ydl099w (Bug1). In addition, Grh1 interacts with the Sec23/24 component of the COPII coat. Neither Grh1 nor Bug1 are essential for growth, but biochemical assays and genetic interactions with known mediators of vesicle tethering (Uso1 and Ypt1) suggest that the Grh1-Bug1 complex contributes to a redundant network of interactions that mediates consumption of COPII vesicles and formation of the cis-Golgi.
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What OpenQuestion holds
Registered trials
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.