ArticleMolecular biology of the cell2023
The Arf-GAP Age2 localizes to the late-Golgi via a conserved amphipathic helix.
Article in Molecular biology of the cell, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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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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Who cites it
8 citing papers in PubMed, 6 citations in OpenAlex.
- Avl9 defines a family of DENN domain GTPase-activating proteins.The Journal of cell biology · 2026Article
- Avl9 defines a family of GTPase-activating proteins that regulate diverse cell biological functions.bioRxiv : the preprint server for biology · 2026Article
- ARF GTPases Function at the Golgi.Sub-cellular biochemistry · 2026Review
- Cisternal Maturation of the Golgi Apparatus in Budding Yeast.Sub-cellular biochemistry · 2026Review
- Structural basis for Rab6 activation by the Ric1-Rgp1 complex.Nature communications · 2024Article
- Regulation of yeast polarized exocytosis by phosphoinositide lipids.Cellular and molecular life sciences : CMLS · 2024Review
- 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
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2 authors at 1 institution in 1 country.
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Abstract
Arf GTPases are central regulators of the Golgi complex, which serves as the nexus of membrane-trafficking pathways in eukaryotic cells. Arf proteins recruit dozens of effectors to modify membranes, sort cargos, and create and tether transport vesicles, and are therefore essential for orchestrating Golgi trafficking. The regulation of Arf activity is controlled by the action of Arf-GEFs which activate via nucleotide exchange, and Arf-GAPs which inactivate via nucleotide hydrolysis. The localization dynamics of Arf GTPases and their Arf-GAPs during Golgi maturation have not been reported. Here we use the budding yeast model to examine the temporal localization of the Golgi Arf-GAPs. We also determine the mechanisms used by the Arf-GAP Age2 to localize to the Golgi. We find that the catalytic activity of Age2 and a conserved sequence in the unstructured C-terminal domain of Age2 are both required for Golgi localization. This sequence is predicted to form an amphipathic helix and mediates direct binding of Age2 to membranes in vitro. We also report the development of a probe for sensing active Arf1 in living cells and use this probe to characterize the temporal dynamics of Arf1 during Golgi maturation.
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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.