BEN3/BIG2 ARF GEF is Involved in Brefeldin A-Sensitive Trafficking at the trans-Golgi Network/Early Endosome in Arabidopsis thaliana
Language English Country Japan Media print
Document type Journal Article
PubMed
29016942
DOI
10.1093/pcp/pcx118
PII: 4086060
Knihovny.cz E-resources
- Keywords
- ARF GEF, Arabidopsis, Auxin, Brefeldin A, PIN-FORMED1, trans-Golgi network,
- MeSH
- ADP-Ribosylation Factors genetics metabolism MeSH
- Alleles MeSH
- Arabidopsis drug effects metabolism MeSH
- Brefeldin A pharmacology MeSH
- Cell Membrane drug effects metabolism MeSH
- Endosomes drug effects metabolism MeSH
- Phenotype MeSH
- Cloning, Molecular MeSH
- Cell Compartmentation MeSH
- Codon, Nonsense genetics MeSH
- Arabidopsis Proteins genetics metabolism MeSH
- Seedlings drug effects growth & development MeSH
- trans-Golgi Network drug effects metabolism MeSH
- Protein Transport drug effects MeSH
- Guanine Nucleotide Exchange Factors metabolism MeSH
- Green Fluorescent Proteins metabolism MeSH
- Publication type
- Journal Article MeSH
- Names of Substances
- ADP-Ribosylation Factors MeSH
- big2 protein Arabidopsis MeSH Browser
- Brefeldin A MeSH
- Codon, Nonsense MeSH
- Arabidopsis Proteins MeSH
- Guanine Nucleotide Exchange Factors MeSH
- Green Fluorescent Proteins MeSH
Membrane traffic at the trans-Golgi network (TGN) is crucial for correctly distributing various membrane proteins to their destination. Polarly localized auxin efflux proteins, including PIN-FORMED1 (PIN1), are dynamically transported between the endosomes and the plasma membrane (PM) in the plant cells. The intracellular trafficking of PIN1 protein is sensitive to the fungal toxin brefeldin A (BFA), which is known to inhibit guanine nucleotide exchange factors for ADP ribosylation factors (ARF GEFs) such as GNOM. However, the molecular details of the BFA-sensitive trafficking pathway have not been fully revealed. In a previous study, we identified an Arabidopsis mutant BFA-visualized endocytic trafficking defective 3 (ben3) which exhibited reduced sensitivity to BFA in terms of BFA-induced intracellular PIN1 agglomeration. Here, we show that BEN3 encodes a member of BIG family ARF GEFs, BIG2. BEN3/BIG2 tagged with fluorescent proteins co-localized with markers for the TGN/early endosome (EE). Inspection of conditionally induced de novo synthesized PIN1 confirmed that its secretion to the PM is BFA sensitive, and established BEN3/BIG2 as a crucial component of this BFA action at the level of the TGN/EE. Furthermore, ben3 mutation alleviated BFA-induced agglomeration of another TGN-localized ARF GEF, BEN1/MIN7. Taken together, our results suggest that BEN3/BIG2 is an ARF GEF component, which confers BFA sensitivity to the TGN/EE in Arabidopsis.
Department of Biological Science Graduate School of Science Osaka University Osaka 560 0043 Japan
Institute of Science and Technology Austria 3400 Klosterneuburg Austria
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