ArticleGenetics1999
Genetic interactions in yeast between Ypt GTPases and Arf guanine nucleotide exchangers.
Article in Genetics, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 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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Who cites it
47 citing papers in PubMed, 84 citations in OpenAlex.
- Structural insight into an Arl1-ArfGEF complex involved in Golgi recruitment of a GRIP-domain golgin.Nature communications · 2024Article
- Cellular Protein Trafficking: A New Player in Low-Temperature Response Pathway.Plants (Basel, Switzerland) · 2022Review
- Rab22a regulates the establishment of epithelial polarity.Small GTPases · 2021Article
- Arf1 directly recruits the Pik1-Frq1 PI4K complex to regulate the final stages of Golgi maturation.Molecular biology of the cell · 2021Article
- Ypt/Rab GTPases and their TRAPP GEFs at the Golgi.FEBS letters · 2019Review
- Ancient complement and lineage-specific evolution of the Sec7 ARF GEF proteins in eukaryotes.Molecular biology of the cell · 2019Article
- ARF GTPases and their GEFs and GAPs: concepts and challenges.Molecular biology of the cell · 2019Review
- Action of Arl1 GTPase and golgin Imh1 in Ypt6-independent retrograde transport from endosomes to the trans-Golgi network.Molecular biology of the cell · 2019Article
- Highly conserved motifs within the large Sec7 ARF guanine nucleotide exchange factor GBF1 target it to the Golgi and are critical for GBF1 activity.American journal of physiology. Cell physiology · 2018Article
- Nucleotide Binding to ARL2 in the TBCD∙ARL2∙β-Tubulin Complex Drives Conformational Changes in β-Tubulin.Journal of molecular biology · 2017Article
- Autophagy in Saccharomyces cerevisiae requires the monomeric GTP-binding proteins, Arl1 and Ypt6.Autophagy · 2016Article
- Structural Insights into Arl1-Mediated Targeting of the Arf-GEF BIG1 to the trans-Golgi.Cell reports · 2016Article
- Regulation of Golgi Cisternal Progression by Ypt/Rab GTPases.Developmental cell · 2016Article
- Ypt/Rab GTPases: principles learned from yeast.Critical reviews in biochemistry and molecular biology · 2015Review
- Four GTPases differentially regulate the Sec7 Arf-GEF to direct traffic at the trans-golgi network.Developmental cell · 2014Article
- Regulating the large Sec7 ARF guanine nucleotide exchange factors: the when, where and how of activation.Cellular and molecular life sciences : CMLS · 2014Review
- Mammalian Mon2/Ysl2 regulates endosome-to-Golgi trafficking but possesses no guanine nucleotide exchange activity toward Arl1 GTPase.Scientific reports · 2013Article
- Regulation of ER-phagy by a Ypt/Rab GTPase module.Molecular biology of the cell · 2013Article
- Regulation of selective autophagy onset by a Ypt/Rab GTPase module.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- GTPase networks in membrane traffic.Annual review of biochemistry · 2012Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 3 institutions in 1 country.
Funding
Abstract
Two families of GTPases, Arfs and Ypt/rabs, are key regulators of vesicular transport. While Arf proteins are implicated in vesicle budding from the donor compartment, Ypt/rab proteins are involved in the targeting of vesicles to the acceptor compartment. Recently, we have shown a role for Ypt31/32p in exit from the yeast trans-Golgi, suggesting a possible function for Ypt/rab proteins in vesicle budding as well. Here we report the identification of a new member of the Sec7-domain family, SYT1, as a high-copy suppressor of a ypt31/32 mutation. Several proteins that belong to the Sec7-domain family, including the yeast Gea1p, have recently been shown to stimulate nucleotide exchange by Arf GTPases. Nucleotide exchange by Arf GTPases, the switch from the GDP- to the GTP-bound form, is thought to be crucial for their function. Sec7p itself has an important role in the yeast secretory pathway. However, its mechanism of action is not yet understood. We show that all members of the Sec7-domain family exhibit distinct genetic interactions with the YPT genes. Biochemical assays demonstrate that, although the homology between the members of the Sec7-domain family is relatively low (20-35%) and limited to a small domain, they all can act as guanine nucleotide exchange factors (GEFs) for Arf proteins, but not for Ypt GTPases. The Sec7-domain of Sec7p is sufficient for this activity. Interestingly, the Sec7 domain activity is inhibited by brefeldin A (BFA), a fungal metabolite that inhibits some of the Arf-GEFs, indicating that this domain is a target for BFA. These results demonstrate that the ability to act as Arf-GEFs is a general property of all Sec7-domain proteins in yeast. The genetic interactions observed between Arf GEFs and Ypt GTPases suggest the existence of a Ypt-Arf GTPase cascade in the secretory pathway.
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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.