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Heimel, Kai
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Heimel, Kai
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Heimel, Kai
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Heimel, K.
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2013Journal Article [["dc.bibliographiccitation.firstpage","4262"],["dc.bibliographiccitation.issue","10"],["dc.bibliographiccitation.journal","The Plant Cell"],["dc.bibliographiccitation.lastpage","4277"],["dc.bibliographiccitation.volume","25"],["dc.contributor.author","Heimel, Kai"],["dc.contributor.author","Freitag, Johannes"],["dc.contributor.author","Hampel, Martin"],["dc.contributor.author","Ast, Julia"],["dc.contributor.author","Boelker, Michael"],["dc.contributor.author","Kaemper, Joerg"],["dc.date.accessioned","2018-11-07T09:18:59Z"],["dc.date.available","2018-11-07T09:18:59Z"],["dc.date.issued","2013"],["dc.description.abstract","The unfolded protein response (UPR) is a conserved eukaryotic signaling pathway regulating endoplasmic reticulum (ER) homeostasis during ER stress, which results, for example, from an increased demand for protein secretion. Here, we characterize the homologs of the central UPR regulatory proteins Hac1 (for Homologous to ATF/CREB1) and Inositol Requiring Enzyme1 in the plant pathogenic fungus Ustilago maydis and demonstrate that the UPR is tightly interlinked with the b mating-type-dependent signaling pathway that regulates pathogenic development. Exact timing of UPR is required for virulence, since premature activation interferes with the b-dependent switch from budding to filamentous growth. In addition, we found crosstalk between UPR and the b target Clampless1 (Clp1), which is essential for cell cycle release and proliferation in planta. The unusual C-terminal extension of the U. maydis Hac1 homolog, Cib1 (for Clp1 interacting bZIP1), mediates direct interaction with Clp1. The interaction between Clp1 and Cib1 promotes stabilization of Clp1, resulting in enhanced ER stress tolerance that prevents deleterious UPR hyperactivation. Thus, the interaction between Cib1 and Clp1 constitutes a checkpoint to time developmental progression and increased secretion of effector proteins at the onset of biotrophic development. Crosstalk between UPR and the b mating-type regulated developmental program adapts ER homeostasis to the changing demands during biotrophy."],["dc.identifier.doi","10.1105/tpc.113.115899"],["dc.identifier.isi","000327723100047"],["dc.identifier.pmid","24179126"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/28530"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Amer Soc Plant Biologists"],["dc.relation.issn","1532-298X"],["dc.relation.issn","1040-4651"],["dc.title","Crosstalk between the Unfolded Protein Response and Pathways That Regulate Pathogenic Development in Ustilago maydis"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]Details DOI PMID PMC WOS2016Journal Article [["dc.bibliographiccitation.firstpage","1135"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","New Phytologist"],["dc.bibliographiccitation.lastpage","1148"],["dc.bibliographiccitation.volume","209"],["dc.contributor.author","Lo Presti, Libera"],["dc.contributor.author","Lopez Diaz, Cristina"],["dc.contributor.author","Turra, David"],["dc.contributor.author","Di Pietro, Antonio"],["dc.contributor.author","Hampel, Martin"],["dc.contributor.author","Heimel, Kai"],["dc.contributor.author","Kahmann, Regine"],["dc.date.accessioned","2018-11-07T10:18:24Z"],["dc.date.available","2018-11-07T10:18:24Z"],["dc.date.issued","2016"],["dc.description.abstract","The maize pathogenic fungus Ustilago maydis experiences endoplasmic reticulum (ER) stress during plant colonization and relies on the unfolded protein response (UPR) to cope with this stress. We identified the U. maydis co-chaperone, designated Dnj1, as part of this conserved cellular response to ER stress Delta dnj1 cells are sensitive to the ER stressor tunicamycin and display a severe virulence defect in maize infection assays. A dnj1 mutant allele unable to stimulate the ATPase activity of chaperones phenocopies the null allele. A Dnj1-mCherry fusion protein localizes in the ER and interacts with the luminal chaperone Bip1. The Fusarium oxysporum Dnj1 ortholog contributes to the virulence of this fungal pathogen in tomato plants. Unlike the human ortholog, F. oxysporum Dnj1 partially rescues the virulence defect of the Ustilago dnj1 mutant. By enabling the fungus to restore ER homeostasis and maintain a high secretory activity, Dnj1 contributes to the establishment of a compatible interaction with the host. Dnj1 orthologs are present in many filamentous fungi, but are absent in budding and fission yeasts. We postulate a conserved and essential role during virulence for this class of co-chaperones."],["dc.identifier.doi","10.1111/nph.13703"],["dc.identifier.isi","000373378000026"],["dc.identifier.pmid","26487566"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/41436"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.relation.issn","1469-8137"],["dc.relation.issn","0028-646X"],["dc.title","A conserved co-chaperone is required for virulence in fungal plant pathogens"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dspace.entity.type","Publication"]]Details DOI PMID PMC WOS