ArticleJournal of cell science2019
Dissection of GTPase-activating proteins reveals functional asymmetry in the COPI coat of budding yeast.
Article in Journal of cell science, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 21 citations in OpenAlex.
- ARF GTPases Function at the Golgi.Sub-cellular biochemistry · 2026Review
- Cargo-selective regulation of clathrin-mediated endocytosis by AMP-activated protein kinase.iScience · 2025Article
- Article
- Arf GTPase-Activating proteins ADAP1 and ARAP1 regulate incorporation of CD63 in multivesicular bodies.Biology open · 2024Article
- The Arf-GAP Age2 localizes to the late-Golgi via a conserved amphipathic helix.Molecular biology of the cell · 2023Article
- Arf1 coordinates fatty acid metabolism and mitochondrial homeostasis.Nature cell biology · 2023Article
- The Arf-GAP Age2 localizes to the late-Golgi via a conserved amphipathic helix.bioRxiv : the preprint server for biology · 2023Article
- STED imaging of endogenously tagged ARF GTPases reveals their distinct nanoscale localizations.The Journal of cell biology · 2023Article
- An interaction between β'-COP and the ArfGAP, Glo3, maintains post-Golgi cargo recycling.The Journal of cell biology · 2023Article
- Article
- The p24 Complex Contributes to Specify Arf1 for COPI Coat Selection.International journal of molecular sciences · 2021Article
- AP-1 Recruits SMAP-1/SMAPs to the trans-Golgi Network to Promote Sorting in Polarized Epithelia.Frontiers in cell and developmental biology · 2021Article
- The Glo3 GAP crystal structure supports the molecular niche model for ArfGAPs in COPI coats.Advances in biological regulation · 2021Article
- AP-3 vesicle uncoating occurs after HOPS-dependent vacuole tethering.The EMBO journal · 2020Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Arf GTPase controls formation of the COPI vesicle coat. Recent structural models of COPI revealed the positioning of two Arf1 molecules in contrasting molecular environments. Each of these pockets for Arf1 is expected to also accommodate an Arf GTPase-activating protein (ArfGAP). Structural evidence and protein interactions observed between isolated domains indirectly suggest that each niche preferentially recruits one of the two ArfGAPs known to affect COPI, i.e. Gcs1/ArfGAP1 and Glo3/ArfGAP2/3, although only partial structures are available. The functional role of the unique non-catalytic domain of either ArfGAP has not been integrated into the current COPI structural model. Here, we delineate key differences in the consequences of triggering GTP hydrolysis through the activity of one versus the other ArfGAP. We demonstrate that Glo3/ArfGAP2/3 specifically triggers Arf1 GTP hydrolysis impinging on the stability of the COPI coat. We show that the Snf1 kinase complex, the yeast homologue of AMP-activated protein kinase (AMPK), phosphorylates the region of Glo3 that is crucial for this effect and, thereby, regulates its function in the COPI-vesicle cycle. Our results revise the model of ArfGAP function in the molecular context of COPI.This article has an associated First Person interview with the first author of the paper.
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