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Plant Cell Advance Online Publication
Published on December 21, 2007; 10.1105/tpc.107.054288

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Received July 17, 2007
Returned for revision November 11, 2007
Accepted November 16, 2007

P-Glycoprotein4 Displays Auxin Efflux Transporter–Like Action in Arabidopsis Root Hair Cells and Tobacco Cells

Misuk Cho 1, Sang Ho Lee 1, and Hyung-Taeg Cho 2*

1 Department of Biology, Chungnam National University, Daejeon 305-764, Korea
2 Department of Biology, Chungnam National University, Daejeon 305-764, Korea; Environmental Biotechnology National Core Research Center, Gyeongsang National University, Jinju 660-701, Korea

* To whom correspondence should be addressed. E-mail: htcho{at}cnu.ac.kr.

ATP binding cassette (ABC) transporters transport diverse substrates across membranes in various organisms. However, plant ABC transporters have only been scantily characterized. By taking advantage of the auxin-sensitive Arabidopsis thaliana root hair cell and tobacco (Nicotiana tabacum) suspension cell systems, we show here that Arabidopsis P-glycoprotein4 (PGP4) displays auxin efflux activity in plant cells. Root hair cell–specific overexpression of PGP4 (PGP4ox) and known auxin efflux transporters, such as PGP1, PGP19, and PIN-FORMEDs, decreased root hair elongation, whereas overexpression of the influx transporter AUXIN-RESISTANT1 enhanced root hair length. PGP4ox-mediated root hair shortening was rescued by the application of auxin or an auxin efflux inhibitor. These results indicate that the increased auxin efflux activity conferred by PGP4 reduces auxin levels in the root hair cell and consequently inhibits root hair elongation. PGP4ox in tobacco suspension cells also increased auxin efflux. PGP4 proteins were targeted to the plasma membrane of Arabidopsis root hair cells and tobacco cells without any clear subcellular polarity. Brefeldin A partially interfered with the trafficking of PGP4 reversibly, and this was rescued by pretreatment with auxin. These results suggest that PGP4 is an auxin efflux transporter in plants and that its trafficking to the plasma membrane involves both BFA-sensitive and -insensitive pathways.






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