ArticleiScience2020
Dynamic Capture and Release of Endoplasmic Reticulum Exit Sites by Golgi Stacks in Arabidopsis.
Article in iScience, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 19 citations in OpenAlex.
- The Golgi vesicle tether p115 can bind directly to the ER exit site organiser Sec16A.Journal of cell science · 2026Article
- Interaction with COPII Member SAR1 Is Critical for the Delivery ofPlants (Basel, Switzerland) · 2026Article
- Plant Golgi and GECCO: The Universality of ER-Golgi Interface.Sub-cellular biochemistry · 2026Review
- Plant-specific tail-anchored coiled-coil protein MAG3 stabilizes Golgi-associated ERESs to facilitate protein exit from the ER.Communications biology · 2025Article
- ER-to-Golgi trafficking through a dynamic intermediate cis-Golgi tubular network in Arabidopsis.Nature cell biology · 2025Article
- Myotubularin 2 interacts with SEC23A and negatively regulates autophagy at ER exit sites in Arabidopsis.Autophagy · 2025Article
- The secretory pathway in Tetrahymena is organized for efficient constitutive secretion at ciliary pockets.iScience · 2024Article
- Article
- A century journey of organelles research in the plant endomembrane system.The Plant cell · 2024Review
- Spatiotemporal dissection of the Golgi apparatus and the ER-Golgi intermediate compartment in budding yeast.eLife · 2024Article
- Molecular mechanisms of endomembrane trafficking in plants.The Plant cell · 2022Review
- A rich and bountiful harvest: Key discoveries in plant cell biology.The Plant cell · 2022Review
- The Golgi Apparatus and its Next-Door Neighbors.Frontiers in cell and developmental biology · 2022Review
- An Update on the Key Factors Required for Plant Golgi Structure Maintenance.Frontiers in plant science · 2022Review
- Differentiation of Trafficking Pathways at Golgi Entry Core Compartments and Post-Golgi Subdomains.Frontiers in plant science · 2020Review
Corrections and comments
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Authors and funding
4 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Protein transport from the endoplasmic reticulum (ER) to Golgi stacks is mediated by the coat protein complex COPII, which is assembled at an ER subdomain called ER exit site (ERES). However, the dynamic relationship between ERESs and Golgi stacks is unknown. Here, we propose a dynamic capture-and-release model of ERESs by Golgi stacks in Arabidopsis thaliana. Using variable-angle epifluorescence microscopy with high-temporal-resolution imaging, COPII-component-bound ERESs were detected as punctate structures with sizes of 300-500 nm. Some punctate ERESs are distributed on ER tubules and sheet rims, whereas others gather around a Golgi stack in an ER-network cavity to form a beaded-ring structure. Free ERESs that wander into an ER cavity are captured by a Golgi stack in a cytoskeleton-independent manner. Then, they are released by the Golgi stack for recycling. The dynamic ERES cycling might contribute to efficient transfer of de novo synthesized cargo proteins from the ER to Golgi stacks.
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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.