BEN3/BIG2 ARF GEF is Involved in Brefeldin A-Sensitive Trafficking at the trans-Golgi Network/Early Endosome in Arabidopsis thaliana
Jazyk angličtina Země Japonsko Médium print
Typ dokumentu časopisecké články
PubMed
29016942
DOI
10.1093/pcp/pcx118
PII: 4086060
Knihovny.cz E-zdroje
- Klíčová slova
- ARF GEF, Arabidopsis, Auxin, Brefeldin A, PIN-FORMED1, trans-Golgi network,
- MeSH
- ADP-ribosylační faktory genetika metabolismus MeSH
- alely MeSH
- Arabidopsis účinky léků metabolismus MeSH
- brefeldin A farmakologie MeSH
- buněčná membrána účinky léků metabolismus MeSH
- endozomy účinky léků metabolismus MeSH
- fenotyp MeSH
- klonování DNA MeSH
- kompartmentace buňky MeSH
- nesmyslný kodon genetika MeSH
- proteiny huseníčku genetika metabolismus MeSH
- semenáček účinky léků růst a vývoj MeSH
- trans-Golgiho síť účinky léků metabolismus MeSH
- transport proteinů účinky léků MeSH
- výměnné faktory guaninnukleotidů metabolismus MeSH
- zelené fluorescenční proteiny metabolismus MeSH
- Publikační typ
- časopisecké články MeSH
- Názvy látek
- ADP-ribosylační faktory MeSH
- big2 protein Arabidopsis MeSH Prohlížeč
- brefeldin A MeSH
- nesmyslný kodon MeSH
- proteiny huseníčku MeSH
- výměnné faktory guaninnukleotidů MeSH
- zelené fluorescenční proteiny 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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