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An LRR receptor kinase controls ABC transporter substrate preferences during plant growth-defense decisions

Affiliation
University of Fribourg, Department of Biology, Switzerland
Aryal, Bibek;
Affiliation
University of Fribourg, Department of Biology, Switzerland ; Present address: Department of Forest Genetics and Plant Physiology, Umea Plant Science Center, Umea , Sweden
Xia, Jian;
Affiliation
University of Fribourg, Department of Biology, Switzerland
Hu, Zehan;
Affiliation
University of Fribourg, Department of Biology, Switzerland
Stumpe, Michael;
Affiliation
University of Fribourg, Department of Biology, Switzerland
Tsering, Tashi;
Affiliation
University of Fribourg, Department of Biology, Switzerland
Liu, Jie;
Affiliation
University of Fribourg, Department of Biology, Switzerland
Huynh, John;
Affiliation
College of Life Sciences, Ritsumeikan University, Japan
Fukao, Yoichiro;
Affiliation
Universität Tübingen, Zentrum für Molekularbiologie der Pflanzen, Pflanzenphysiologie, Germany
Glöckner, Nina;
Affiliation
ETH Zürich, Department of Biology, Switzerland
Huang, Hsin-Yao;
Affiliation
ETH Zürich, Department of Biology, Switzerland
Sáncho-Andrés, Gloria;
Affiliation
Polish Academy of Sciences, Department of Plant Molecular Physiology, Institute of Bioorganic Chemistry, Poland
Pakula, Konrad;
Affiliation
Leibniz Institute of Plant Biochemistry, Department Molecular Signal Processing, Germany
Ziegler, Joerg;
GND
1058136283
Affiliation
present adress: Julius Kühn-Institute (JKI), Institute for Ecological Chemistry, Plant Analysis and Stored Product Protection, Germany ; Leibniz Institute of Plant Biochemistry, Department Biochemistry of Plant Interactions, Germany
Gorzolka, Karin;
Affiliation
Mendel Centre for Plant Genomics and Proteomics Masaryk University, Czech Republic
Zwiewka, Marta;
Affiliation
Mendel Centre for Plant Genomics and Proteomics Masaryk University, Czech Republic
Nodzynski, Tomasz;
Affiliation
Universität Tübingen, Zentrum für Molekularbiologie der Pflanzen, Pflanzenphysiologie, Germany
Harter, Klaus;
Affiliation
ETH Zürich, Department of Biology, Switzerland
Sánchez-Rodríguez, Clara;
Affiliation
Polish Academy of Sciences, Department of Plant Molecular Physiology, Institute of Bioorganic Chemistry, Poland
Jasiński, Michał;
Affiliation
Leibniz Institute of Plant Biochemistry, Department Biochemistry of Plant Interactions, Germany
Rosahl, Sabine;
Affiliation
University of Fribourg, Department of Biology, Switzerland
Geisler, Markus M.

The exporter of the auxin precursor indole-3-butyric acid (IBA), ABCG36/PDR8/PEN3, from the model plant
Arabidopsis has recently been proposed to also function in the transport of the phytoalexin camalexin. Based
on these bonafide substrates, it has been suggested that ABCG36 functions at the interface between growth
and defense.
Here, we provide evidence that ABCG36 catalyzes the direct, ATP-dependent export of camalexin across the
plasma membrane. We identify the leucine-rich repeat receptor kinase, QIAN SHOU KINASE1 (QSK1), as a
functional kinase that physically interacts with and phosphorylates ABCG36. Phosphorylation of ABCG36
by QSK1 unilaterally represses IBA export, allowing camalexin export by ABCG36 conferring pathogen resistance.
As a consequence, phospho-dead mutants of ABCG36, as well as qsk1 and abcg36 alleles, are hypersensitive
to infection with the root pathogen Fusarium oxysporum, caused by elevated fungal progression.
Our findings indicate a direct regulatory circuit between a receptor kinase and an ABC transporter that functions
to control transporter substrate preference during plant growth and defense balance decisions.

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