title: Immobilized Subpopulations of Leaf Epidermal Mitochondria Mediate PENETRATION2-Dependent Pathogen Entry Control in Arabidopsis.
abstract: The atypical myrosinase PENETRATION2 (PEN2) is required for broad-spectrum invasion resistance to filamentous plant pathogens. Previous localization studies suggested PEN2-GFP association with peroxisomes. Here, we show that PEN2 is a tail-anchored protein with dual-membrane targeting to peroxisomes and mitochondria and that PEN2 has the capacity to form homo-oligomer complexes. We demonstrate pathogen-induced recruitment and immobilization of mitochondrial subpopulations at sites of attempted fungal invasion and show that mitochondrial arrest is accompanied by peripheral accumulation of GFP-tagged PEN2. PEN2 substrate production by the cytochrome P450 monooxygenase CYP81F2 is localized to the surface of the endoplasmic reticulum, which focally reorganizes close to the immobilized mitochondria. Exclusive targeting of PEN2 to the outer membrane of mitochondria complements the pen2 mutant phenotype, corroborating the functional importance of the mitochondrial PEN2 protein subpool for controlled local production of PEN2 hydrolysis products at subcellular plant-microbe interaction domains. Moreover, live-cell imaging shows that mitochondria arrested at these domains exhibit a pathogen-induced redox imbalance, which may lead to the production of intracellular signals.
authors.affiliation: Department of Plant Cell Biology, Albrecht-von-Haller-Institute, Georg-August-University Göttingen, 37077 Göttingen, Germany The Sainsbury Laboratory, Norwich NR4 7UH, United Kingdom.
authors.forename: Rene
authors.identifier: http://orcid.org/0000-0001-5056-5323
authors.initials: R
authors.lastname: Fuchs
authors.affiliation: Department of Plant Cell Biology, Albrecht-von-Haller-Institute, Georg-August-University Göttingen, 37077 Göttingen, Germany The Sainsbury Laboratory, Norwich NR4 7UH, United Kingdom.
authors.forename: Michaela
authors.identifier: http://orcid.org/0000-0002-3524-3104
authors.initials: M
authors.lastname: Kopischke
authors.affiliation: Department of Plant Cell Biology, Albrecht-von-Haller-Institute, Georg-August-University Göttingen, 37077 Göttingen, Germany The Sainsbury Laboratory, Norwich NR4 7UH, United Kingdom.
authors.forename: Christine
authors.initials: C
authors.lastname: Klapprodt
authors.affiliation: Martin-Luther-Universität Halle-Wittenberg, Universitätsbiozentrum, 06120 Halle, Germany.
authors.forename: Gerd
authors.initials: G
authors.lastname: Hause
authors.affiliation: University of Bonn, INRES-Chemical Signalling, 53113 Bonn, Germany.
authors.forename: Andreas J
authors.identifier: http://orcid.org/0000-0001-8144-4364
authors.initials: AJ
authors.lastname: Meyer
authors.affiliation: University of Bonn, INRES-Chemical Signalling, 53113 Bonn, Germany.
authors.forename: Markus
authors.identifier: http://orcid.org/0000-0003-0796-8308
authors.initials: M
authors.lastname: Schwarzländer
authors.affiliation: Department of Plant Sciences, University of Oxford, Oxford OX1 3RB, United Kingdom.
authors.forename: Mark D
authors.identifier: http://orcid.org/0000-0002-8942-6897
authors.initials: MD
authors.lastname: Fricker
authors.affiliation: Department of Plant Cell Biology, Albrecht-von-Haller-Institute, Georg-August-University Göttingen, 37077 Göttingen, Germany The Sainsbury Laboratory, Norwich NR4 7UH, United Kingdom vlipka@gwdg.de.
authors.forename: Volker
authors.initials: V
authors.lastname: Lipka
mesh_terms: D000595:Amino Acid Sequence; D017360:Arabidopsis / Q000378:metabolism* / Q000382:microbiology*; D029681:Arabidopsis Proteins / Q000737:chemistry / Q000378:metabolism*; D001203:Ascomycota / Q000472:pathogenicity*; D060467:Disease Resistance; D004721:Endoplasmic Reticulum / Q000378:metabolism; D049452:Green Fluorescent Proteins / Q000378:metabolism; D054884:Host-Pathogen Interactions; D008928:Mitochondria / Q000378:metabolism*; D051336:Mitochondrial Membranes / Q000378:metabolism; D008969:Molecular Sequence Data; D009699:N-Glycosyl Hydrolases / Q000737:chemistry / Q000378:metabolism*; D010084:Oxidation-Reduction; D020675:Peroxisomes / Q000378:metabolism; D010935:Plant Diseases / Q000382:microbiology; D019441:Plant Epidermis / Q000378:metabolism*; D018515:Plant Leaves / Q000378:metabolism*; D055503:Protein Multimerization; D013347:Subcellular Fractions / Q000378:metabolism; D013379:Substrate Specificity
chemical_list: D029681:Arabidopsis Proteins; D049452:Green Fluorescent Proteins; D009699:N-Glycosyl Hydrolases; C505663:PEN2 protein, Arabidopsis