ReviewTraffic (Copenhagen, Denmark)2010
The yeast GRASP Grh1 colocalizes with COPII and is dispensable for organizing the secretory pathway.
Review in Traffic (Copenhagen, Denmark), 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 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
44 citing papers in PubMed, 78 citations in OpenAlex.
- The role of N-terminal acetylation on biomolecular condensation.Communications chemistry · 2026Article
- Close-up of vesicular ER exit sites by volume electron imaging using FIB-SEM.The Journal of cell biology · 2026Article
- Phosphorylation of Golgin Imh1 by AMPK/Snf1 compromises Golgi compartmentalization by releasing Arl1-Imh1 axis.Molecular biology of the cell · 2025Article
- Spatiotemporal dissection of the Golgi apparatus and the ER-Golgi intermediate compartment in budding yeast.eLife · 2024Article
- Yeast cell death pathway requiring AP-3 vesicle trafficking leads to vacuole/lysosome membrane permeabilization.Cell reports · 2022Article
- Unconventional Protein Secretion in Brain Tumors Biology: Enlightening the Mechanisms for Tumor Survival and Progression.Frontiers in cell and developmental biology · 2022Review
- GRASP55 restricts early-stage autophagy and regulates spatial organization of the early secretory network.Biology open · 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
- ER arrival sites associate with ER exit sites to create bidirectional transport portals.The Journal of cell biology · 2020Article
- Golgin45-Syntaxin5 Interaction Contributes to Structural Integrity of the Golgi Stack.Scientific reports · 2019Article
- Maturation-driven transport and AP-1-dependent recycling of a secretory cargo in the Golgi.The Journal of cell biology · 2019Article
- The yeast GRASP Grh1 displays a high polypeptide backbone mobility along with an amyloidogenic behavior.Scientific reports · 2018Article
- Stochastic Model of Maturation and Vesicular Exchange in Cellular Organelles.Biophysical journal · 2018Article
- Budding Yeast Has a Minimal Endomembrane System.Developmental cell · 2018Article
- The Golgin protein Coy1 functions in intra-Golgi retrograde transport and interacts with the COG complex and Golgi SNAREs.Molecular biology of the cell · 2017Article
- Three-dimensional and immune electron microscopic analysis of the secretory pathway in Saccharomyces cerevisiae.Histochemistry and cell biology · 2016Article
- ER arrival sites for COPI vesicles localize to hotspots of membrane trafficking.The EMBO journal · 2016Article
- Secreted Acb1 Contributes to the Yeast-to-Hypha Transition in Cryptococcus neoformans.Applied and environmental microbiology · 2016Article
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 1 institution in 1 country.
Funding
Abstract
In mammalian cells, the 'Golgi reassembly and stacking protein' (GRASP) family has been implicated in Golgi stacking, but the broader functions of GRASP proteins are still unclear. The yeast Saccharomyces cerevisiae contains a single non-essential GRASP homolog called Grh1. However, Golgi cisternae in S. cerevisiae are not organized into stacks, so a possible structural role for Grh1 has been difficult to test. Here, we examined the localization and function of Grh1 in S. cerevisiae and in the related yeast Pichia pastoris, which has stacked Golgi cisternae. In agreement with earlier studies indicating that Grh1 interacts with coat protein II (COPII) vesicle coat proteins, we find that Grh1 colocalizes with COPII at transitional endoplasmic reticulum (tER) sites in both yeasts. Deletion of P. pastoris Grh1 had no obvious effect on the structure of tER-Golgi units. To test the role of S. cerevisiae Grh1, we exploited the observation that inhibiting ER export in S. cerevisiae generates enlarged tER sites that are often associated with the cis Golgi. This tER-Golgi association was preserved in the absence of Grh1. The combined data suggest that Grh1 acts early in the secretory pathway, but is dispensable for the organization of secretory compartments.
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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.