Journal
PLANT AND CELL PHYSIOLOGY
Volume 55, Issue 4, Pages 737-749Publisher
OXFORD UNIV PRESS
DOI: 10.1093/pcp/pct196
Keywords
Arabidopsis thaliana; Auxin; Embryogenesis; Exocytosis; PIN-FORMED
Categories
Funding
- Ministry of Education, Culture, Sports, Science and Technology (MEXT)
- Japan Society for the Promotion of Science (JSPS) KAKENHI [23012026, 23770147]
- International Human Frontier Science Program Organization (HFSP CDA)
- Vienna Science and Technology Fund (WWTF)
- European Research Council [ERC-2011-StG-20101109-PSDP]
- European Social Fund [CZ.1.07/2.3.00/20.0043]
- Czech Science Foundation GACR [GA13-40637S]
- state budget of the Czech Republic [CZ.1.07/2.3.00/30.0009]
- Grants-in-Aid for Scientific Research [19060005, 25114504, 23770147, 25113006, 23012026] Funding Source: KAKEN
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Correct positioning of membrane proteins is an essential process in eukaryotic organisms. The plant hormone auxin is distributed through intercellular transport and triggers various cellular responses. Auxin transporters of the PIN-FORMED (PIN) family localize asymmetrically at the plasma membrane (PM) and mediate the directional transport of auxin between cells. A fungal toxin, brefeldin A (BFA), inhibits a subset of guanine nucleotide exchange factors for ADP-ribosylation factor small GTPases (ARF GEFs) including GNOM, which plays a major role in localization of PIN1 predominantly to the basal side of the PM. The Arabidopsis genome encodes 19 ARF-related putative GTPases. However, ARF components involved in PIN1 localization have been genetically poorly defined. Using a fluorescence imaging-based forward genetic approach, we identified an Arabidopsis mutant, bfa-visualized exocytic trafficking defective1 (bex1), in which PM localization of PIN1-green fluorescent protein (GFP) as well as development is hypersensitive to BFA. We found that in bex1 a member of the ARF1 gene family, ARF1A1C, was mutated. ARF1A1C localizes to the trans-Golgi network/early endosome and Golgi apparatus, acts synergistically to BEN1/MIN7 ARF GEF and is important for PIN recycling to the PM. Consistent with the developmental importance of PIN proteins, functional interference with ARF1 resulted in an impaired auxin response gradient and various developmental defects including embryonic patterning defects and growth arrest. Our results show that ARF1A1C is essential for recycling of PIN auxin transporters and for various auxin-dependent developmental processes.
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