ArticleCell reports2022
Structural basis for activation of Arf1 at the Golgi complex.
Article in Cell reports, 2022. 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, 23 citations in OpenAlex.
- ARMH3 acts as a central scaffold at the Golgi/TGN through interactions with Arl5, GBF1, and PI4KB.The Journal of biological chemistry · 2026Article
- Host protein ARF1 is a proviral factor for SARS-CoV-2 and a candidate broad-spectrum therapeutic target.Nature communications · 2025Article
- A large-scale curated and filterable dataset for cryo-EM foundation model pre-training.Scientific data · 2025Article
- Structural insights into traffic through the Golgi complex.Current opinion in cell biology · 2025Review
- Crosstalk between dysregulated amino acid sensing and glucose and lipid metabolism in colorectal cancer.Frontiers in oncology · 2025Review
- Structural basis for Rab6 activation by the Ric1-Rgp1 complex.Nature communications · 2024Article
- Structural basis for Rab6 activation by the Ric1-Rgp1 complex.bioRxiv : the preprint server for biology · 2024Article
- Sec7 regulatory domains scaffold autoinhibited and active conformations.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Structural insight into an Arl1-ArfGEF complex involved in Golgi recruitment of a GRIP-domain golgin.Nature communications · 2024Article
- The Arf-GAP Age2 localizes to the late-Golgi via a conserved amphipathic helix.Molecular biology of the cell · 2023Article
- The Arf-GAP Age2 localizes to the late-Golgi via a conserved amphipathic helix.bioRxiv : the preprint server for biology · 2023Article
- Article
- Kinetics of Arf1 inactivation regulates Golgi organisation and function in non-adherent fibroblasts.Biology open · 2023Article
- The Arf-GEF GBF1 undergoes multi-domain structural shifts to activate Arf at the Golgi.Frontiers in cell and developmental biology · 2023Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The Golgi complex is the central sorting station of the eukaryotic secretory pathway. Traffic through the Golgi requires activation of Arf guanosine triphosphatases that orchestrate cargo sorting and vesicle formation by recruiting an array of effector proteins. Arf activation and Golgi membrane association is controlled by large guanine nucleotide exchange factors (GEFs) possessing multiple conserved regulatory domains. Here we present cryoelectron microscopy (cryoEM) structures of full-length Gea2, the yeast paralog of the human Arf-GEF GBF1, that reveal the organization of these regulatory domains and explain how Gea2 binds to the Golgi membrane surface. We find that the GEF domain adopts two different conformations compatible with different stages of the Arf activation reaction. The structure of a Gea2-Arf1 activation intermediate suggests that the movement of the GEF domain primes Arf1 for membrane insertion upon guanosine triphosphate binding. We propose that conformational switching of Gea2 during the nucleotide exchange reaction promotes membrane insertion of Arf1.
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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 Socratic graph.