ArticleBiology open2015
The ArfGAP2/3 Glo3 and ergosterol collaborate in transport of a subset of cargoes.
Article in Biology open, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 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
9 citing papers in PubMed.
- Fluorescent organelle markers in Cryptococcus neoformans: a versatile toolkit for live-cell subcellular localization.Genetics · 2026Article
- Fluorescent organelle markers inbioRxiv : the preprint server for biology · 2026Article
- Article
- Cyclo(Pro-Tyr) elicits conserved cellular damage in fungi by targeting the [HCommunications biology · 2024Article
- Acquired Triazole Resistance Alters Pathogenicity-Associated Features inJournal of fungi (Basel, Switzerland) · 2023Article
- Article
- Synergistic and antagonistic drug interactions in the treatment of systemic fungal infections.eLife · 2020Article
- Asymmetric distribution of glucose transporter mRNA provides a growth advantage in yeast.The EMBO journal · 2019Article
- Article
Corrections and comments
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Proteins reach the plasma membrane through the secretory pathway in which the trans Golgi network (TGN) acts as a sorting station. Transport from the TGN to the plasma membrane is maintained by a number of different pathways that act either directly or via the endosomal system. Here we show that a subset of cargoes depends on the ArfGAP2/3 Glo3 and ergosterol to maintain their proper localization at the plasma membrane. While interfering with neither ArfGAP2/3 activity nor ergosterol biosynthesis individually significantly altered plasma membrane localization of the tryptophan transporter Tat2, the general amino acid permease Gap1 and the v-SNARE Snc1, in a Δglo3 Δerg3 strain those proteins accumulated in internal endosomal structures. Export from the TGN to the plasma membrane and recycling from early endosomes appeared unaffected as the chitin synthase Chs3 that travels along these routes was localized normally. Our data indicate that a subset of proteins can reach the plasma membrane efficiently but after endocytosis becomes trapped in endosomal structures. Our study supports a role for ArfGAP2/3 in recycling from endosomes and in transport to the vacuole/lysosome.
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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.