Evidence map›Paper›PMID 26721862›Full record

ArticleThe Plant cell2016

Immobilized Subpopulations of Leaf Epidermal Mitochondria Mediate PENETRATION2-Dependent Pathogen Entry Control in Arabidopsis.

Rene Fuchs, Michaela Kopischke, Christine Klapprodt, Gerd Hause, Andreas J Meyer, Markus Schwarzländer, Mark D Fricker, Volker Lipka

Abstract read
In one paragraph

Article in The Plant cell, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.

0numbers the graph read from it
0cells of the map it votes in
47citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

47 citing papers in PubMed.

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  17. ER Bodies Are Induced byMolecular plant-microbe interactions : MPMI · 2021
    Article
  18. Metatranscriptomic Comparison of Endophytic and PathogenicMolecular plant-microbe interactions : MPMI · 2021
    Article
  19. Article
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors.

Rene FuchsDepartment of Plant Cell Biology, Albrecht-von-Haller-Institute, Georg-August-University Göttingen, 37077 Göttingen, Germany The Sainsbury Laboratory, Norwich NR4 7UH, United Kingdom.ORCID http://orcid.org/0000-0001-5056-5323
Michaela KopischkeDepartment of Plant Cell Biology, Albrecht-von-Haller-Institute, Georg-August-University Göttingen, 37077 Göttingen, Germany The Sainsbury Laboratory, Norwich NR4 7UH, United Kingdom.ORCID http://orcid.org/0000-0002-3524-3104
Christine KlapprodtDepartment of Plant Cell Biology, Albrecht-von-Haller-Institute, Georg-August-University Göttingen, 37077 Göttingen, Germany The Sainsbury Laboratory, Norwich NR4 7UH, United Kingdom.
Gerd HauseMartin-Luther-Universität Halle-Wittenberg, Universitätsbiozentrum, 06120 Halle, Germany.
Andreas J MeyerUniversity of Bonn, INRES-Chemical Signalling, 53113 Bonn, Germany.ORCID http://orcid.org/0000-0001-8144-4364
Markus SchwarzländerUniversity of Bonn, INRES-Chemical Signalling, 53113 Bonn, Germany.ORCID http://orcid.org/0000-0003-0796-8308
Mark D FrickerDepartment of Plant Sciences, University of Oxford, Oxford OX1 3RB, United Kingdom.ORCID http://orcid.org/0000-0002-8942-6897
Volker LipkaDepartment 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.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

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.

Indexed as

Host-Pathogen InteractionsAmino Acid SequenceArabidopsisArabidopsis ProteinsAscomycotaDisease ResistanceEndoplasmic ReticulumGreen Fluorescent ProteinsMitochondriaMitochondrial MembranesMolecular Sequence DataN-Glycosyl HydrolasesOxidation-ReductionPeroxisomesPlant DiseasesPlant EpidermisArabidopsis ProteinsGreen Fluorescent ProteinsN-Glycosyl HydrolasesPEN2 protein, Arabidopsis

Identifiers

PMID26721862
PMCPMC4746686

What OpenQuestion holds

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.