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Arabidopsis BTB/POZ protein-dependent PENETRATION3 trafficking and disease susceptibility

  • Mao, Hailiang Ume? Plant Science Centre, Department of Plant Physiology, Ume? University, Sweden
  • Aryal, Bibek Department of Biology, Plant Biology, Unit, University of Fribourg, Switzerland
  • Langenecker, Tobias Department of Molecular Biology, Max Planck Institute for Developmental Biology, Tübingen, Germany
  • Hagmann, Jörg Department of Molecular Biology, Max Planck Institute for Developmental Biology, Tübingen, Germany - Computomics GmbH, Tübingen, Germany
  • Geisler, Markus Department of Biology, Plant Biology, Unit, University of Fribourg, Switzerland
  • Grebe, Markus Ume? Plant Science Centre, Department of Plant Physiology, Ume? University, Sweden - Institute of Biochemistry and Biology, Department of Plant Physiology, University of Potsdam, Germany
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    01.11.2017
Published in:
  • Nature Plants. - 2017, vol. 3, no. 11, p. 854
English The outermost cell layer of plant roots (epidermis) constantly encounters environmental challenges. The epidermal outer plasma membrane domain harbours the PENETRATION3 (PEN3)/ABCG36/PDR8 ATP-binding cassette transporter that confers non-host resistance to several pathogens. Here, we show that the Arabidopsis ENDOPLASMIC RETICULUM-ARRESTED PEN3 (EAP3) BTB/POZ-domain protein specifically mediates PEN3 exit from the endoplasmic reticulum and confers resistance to a root-penetrating fungus, providing prime evidence for BTB/POZ- domain protein-dependent membrane trafficking underlying disease resistance.The PENETRATION3 (PEN3/ABCG36/PDR8) ATP-binding cassette transporter of Arabidopsis thaliana is a crucial component of preinvasive defence against some fungal and bacterial non-host pathogens entering by direct penetration1,2,3,4. In above-ground organs, PEN3 is recruited to sites of pathogen attack at the cell surface3,4. In seedling roots, PEN3 polarly localizes to the epidermal outer membrane domain in the absence of pathogens5,6. Root epidermal cells display four major polar plasma membrane domains: the outer domain facing the environment, the inner domain oriented towards the cortical cell layer, the shootward-oriented, apical, and the root tip-oriented, basal, domain6. Proteins in the outer domain that function in regulating the transport of inorganic compounds include, for example, the NIP5;1 boric acid uptake channel7. Factors required for PEN3 and NIP5;1 trafficking from the trans-Golgi network to the outer domain have been identified8,9,10, and exocyst complex components promote polar tethering of several outer domain proteins9,11. However, factors that specifically mediate trafficking of polar outer membrane cargos involved in responses to root-penetrating pathogens remain to be discovered.In a genetic screen for mislocalization of PEN3 fused to green-fluorescent protein (PEN3- GFP) in the root epidermis of seedlings9, we recovered one recessive mutant in which PEN3-GFP localized to a cytoplasmic structure resembling the endoplasmic reticulum (ER) (Fig. 1a–d). This er-arrested pen3-1 (eap3-1) mutation indistinguishably affected localization of PEN3-GFP from that of PEN3-mCherry (Supplementary Fig. 1a,b), which colocalized with the ER-intrinsic chaperone BIP in the eap3-1 mutant (Supplementary Fig. 1c,d), corroborating an ER arrest of PEN3.
Faculty
Faculté des sciences et de médecine
Department
Département de Biologie
Language
  • English
Classification
Biological sciences
License
License undefined
Identifiers
Persistent URL
https://folia.unifr.ch/unifr/documents/306310
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