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The High Osmolarity Glycerol Mitogen-Activated Protein Kinase regulates glucose catabolite repression in filamentous fungi

dc.contributor.authorde Assis, Leandro José
dc.contributor.authorSilva, Lilian Pereira
dc.contributor.authorLiu, Li
dc.contributor.authorSchmitt, Kerstin
dc.contributor.authorValerius, Oliver
dc.contributor.authorBraus, Gerhard H.
dc.contributor.authorRies, Laure Nicolas Annick
dc.contributor.authorGoldman, Gustavo Henrique
dc.date.accessioned2020-10-28T15:11:55Z
dc.date.available2020-10-28T15:11:55Z
dc.date.issued2020de
dc.identifier.urihttp://resolver.sub.uni-goettingen.de/purl?gs-1/17631
dc.description.abstractThe utilization of different carbon sources in filamentous fungi underlies a complex regulatory network governed by signaling events of different protein kinase pathways, including the high osmolarity glycerol (HOG) and protein kinase A (PKA) pathways. This work unraveled cross-talk events between these pathways in governing the utilization of preferred (glucose) and non-preferred (xylan, xylose) carbon sources in the reference fungus Aspergillus nidulans. An initial screening of a library of 103 non-essential protein kinase (NPK) deletion strains identified several mitogen-activated protein kinases (MAPKs) to be important for carbon catabolite repression (CCR). We selected the MAPKs Ste7, MpkB, and PbsA for further characterization and show that they are pivotal for HOG pathway activation, PKA activity, CCR via regulation of CreA cellular localization and protein accumulation, as well as for hydrolytic enzyme secretion. Protein-protein interaction studies show that Ste7, MpkB, and PbsA are part of the same protein complex that regulates CreA cellular localization in the presence of xylan and that this complex dissociates upon the addition of glucose, thus allowing CCR to proceed. Glycogen synthase kinase (GSK) A was also identified as part of this protein complex and shown to potentially phosphorylate two serine residues of the HOG MAPKK PbsA. This work shows that carbon source utilization is subject to cross-talk regulation by protein kinases of different signaling pathways. Furthermore, this study provides a model where the correct integration of PKA, HOG, and GSK signaling events are required for the utilization of different carbon sources.de
dc.description.sponsorshipOpen-Access-Publikationsfonds 2020
dc.language.isoengde
dc.rightsopenAccess
dc.rightsNamensnennung 4.0 International*
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/*
dc.subjectPhosphorylation; Glucose; Protein kinases; Aspergillus nidulans; MAPK signaling cascades; Xylose; Enzyme regulation; Glucose signalingde
dc.subject.ddc570
dc.titleThe High Osmolarity Glycerol Mitogen-Activated Protein Kinase regulates glucose catabolite repression in filamentous fungide
dc.typejournalArticlede
dc.identifier.doi10.1371/journal.pgen.1008996
dc.identifier.doi10.1371/journal.pgen.1008996.g001
dc.identifier.doi10.1371/journal.pgen.1008996.g002
dc.identifier.doi10.1371/journal.pgen.1008996.g003
dc.identifier.doi10.1371/journal.pgen.1008996.g004
dc.identifier.doi10.1371/journal.pgen.1008996.g005
dc.identifier.doi10.1371/journal.pgen.1008996.g006
dc.identifier.doi10.1371/journal.pgen.1008996.g007
dc.identifier.doi10.1371/journal.pgen.1008996.g008
dc.identifier.doi10.1371/journal.pgen.1008996.s001
dc.identifier.doi10.1371/journal.pgen.1008996.s002
dc.identifier.doi10.1371/journal.pgen.1008996.s003
dc.identifier.doi10.1371/journal.pgen.1008996.s004
dc.identifier.doi10.1371/journal.pgen.1008996.s005
dc.identifier.doi10.1371/journal.pgen.1008996.s006
dc.identifier.doi10.1371/journal.pgen.1008996.s007
dc.identifier.doi10.1371/journal.pgen.1008996.r001
dc.identifier.doi10.1371/journal.pgen.1008996.r002
dc.identifier.doi10.1371/journal.pgen.1008996.r003
dc.identifier.doi10.1371/journal.pgen.1008996.r004
dc.type.versionpublishedVersionde
dc.relation.eISSN1553-7404
dc.bibliographicCitation.volume16de
dc.bibliographicCitation.issue8de
dc.bibliographicCitation.firstPage1de
dc.bibliographicCitation.lastPage27de
dc.type.subtypejournalArticle
dc.bibliographicCitation.articlenumbere1008996de
dc.description.statuspeerReviewedde
dc.bibliographicCitation.journalPLOS Geneticsde


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