Uhrig, Joachim F.

[["dc.bibliographiccitation.journal","Frontiers in Molecular Neuroscience"],["dc.bibliographiccitation.volume","14"],["dc.contributor.author","Popova, Blagovesta"],["dc.contributor.author","Wang, Dan"],["dc.contributor.author","Rajavel, Abirami"],["dc.contributor.author","Dhamotharan, Karthikeyan"],["dc.contributor.author","Lázaro, Diana F."],["dc.contributor.author","Gerke, Jennifer"],["dc.contributor.author","Uhrig, Joachim F."],["dc.contributor.author","Hoppert, Michael"],["dc.contributor.author","Outeiro, Tiago Fleming"],["dc.contributor.author","Braus, Gerhard H."],["dc.date.accessioned","2021-06-01T09:42:26Z"],["dc.date.available","2021-06-01T09:42:26Z"],["dc.date.issued","2021"],["dc.description.abstract","Aggregation of α-synuclein (αSyn) into proteinaceous deposits is a pathological hallmark of a range of neurodegenerative diseases including Parkinson’s disease (PD). Numerous lines of evidence indicate that the accumulation of toxic oligomeric and prefibrillar αSyn species may underpin the cellular toxicity and spread of pathology between cells. Therefore, aggregation of αSyn is considered a priority target for drug development, as aggregation inhibitors are expected to reduce αSyn toxicity and serve as therapeutic agents. Here, we used the budding yeast S. cerevisiae as a platform for the identification of short peptides that inhibit αSyn aggregation and toxicity. A library consisting of approximately one million peptide variants was utilized in two high-throughput screening approaches for isolation of library representatives that reduce αSyn-associated toxicity and aggregation. Seven peptides were isolated that were able to suppress specifically αSyn toxicity and aggregation in living cells. Expression of the peptides in yeast reduced the accumulation of αSyn-induced reactive oxygen species and increased cell viability. Next, the peptides were chemically synthesized and probed for their ability to modulate αSyn aggregation in vitro . Two synthetic peptides, K84s and K102s, of 25 and 19 amino acids, respectively, significantly inhibited αSyn oligomerization and aggregation at sub-stoichiometric molar ratios. Importantly, K84s reduced αSyn aggregation in human cells. These peptides represent promising αSyn aggregation antagonists for the development of future therapeutic interventions."],["dc.description.sponsorship","Open-Access-Publikationsfonds 2021"],["dc.identifier.doi","10.3389/fnmol.2021.659926"],["dc.identifier.pmid","33912013"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/17845"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/85254"],["dc.identifier.url","https://mbexc.uni-goettingen.de/literature/publications/420"],["dc.notes.intern","DOI-Import GROB-425"],["dc.notes.intern","Merged from goescholar"],["dc.relation","EXC 2067: Multiscale Bioimaging"],["dc.relation.eissn","1662-5099"],["dc.relation.workinggroup","RG Outeiro (Experimental Neurodegeneration)"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.title","Identification of Two Novel Peptides That Inhibit α-Synuclein Toxicity and Aggregation"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","e1005811"],["dc.bibliographiccitation.issue","8"],["dc.bibliographiccitation.journal","PLoS Pathogens"],["dc.bibliographiccitation.volume","12"],["dc.contributor.author","Couto, Daniel"],["dc.contributor.author","Niebergall, Roda"],["dc.contributor.author","Liang, Xiangxiu"],["dc.contributor.author","Bucherl, Christoph A."],["dc.contributor.author","Sklenar, Jan"],["dc.contributor.author","Macho, Alberto P."],["dc.contributor.author","Ntoukakis, Vardis"],["dc.contributor.author","Derbyshire, Paul"],["dc.contributor.author","Altenbach, Denise"],["dc.contributor.author","Maclean, Dan"],["dc.contributor.author","Robatzek, Silke"],["dc.contributor.author","Uhrig, Joachim F."],["dc.contributor.author","Menke, Frank"],["dc.contributor.author","Zhou, J."],["dc.contributor.author","Zipfel, Cyril"],["dc.date.accessioned","2018-11-07T10:10:42Z"],["dc.date.available","2018-11-07T10:10:42Z"],["dc.date.issued","2016"],["dc.description.abstract","Plants recognize pathogen-associated molecular patterns (PAMPs) via cell surface-localized pattern recognition receptors (PRRs), leading to PRR-triggered immunity (PTI). The Arabidopsis cytoplasmic kinase BIK1 is a downstream substrate of several PRR complexes. How plant PTI is negatively regulated is not fully understood. Here, we identify the protein phosphatase PP2C38 as a negative regulator of BIK1 activity and BIK1-mediated immunity. PP2C38 dynamically associates with BIK1, as well as with the PRRs FLS2 and EFR, but not with the co-receptor BAK1. PP2C38 regulates PAMP-induced BIK1 phosphorylation and impairs the phosphorylation of the NADPH oxidase RBOHD by BIK1, leading to reduced oxidative burst and stomatal immunity. Upon PAMP perception, PP2C38 is phosphorylated on serine 77 and dissociates from the FLS2/EFR-BIK1 complexes, enabling full BIK1 activation. Together with our recent work on the control of BIK1 turnover, this study reveals another important regulatory mechanism of this central immune component."],["dc.identifier.doi","10.1371/journal.ppat.1005811"],["dc.identifier.isi","000383376000041"],["dc.identifier.pmid","27494702"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/14129"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/39911"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Public Library Science"],["dc.relation.issn","1553-7374"],["dc.relation.issn","1553-7366"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","The Arabidopsis Protein Phosphatase PP2C38 Negatively Regulates the Central Immune Kinase BIK1"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","123"],["dc.bibliographiccitation.issue","1-2"],["dc.bibliographiccitation.journal","Plant Molecular Biology"],["dc.bibliographiccitation.lastpage","140"],["dc.bibliographiccitation.volume","95"],["dc.contributor.author","Palm-Forster, Mieder Anthony Thomas"],["dc.contributor.author","Eschen-Lippold, Lennart"],["dc.contributor.author","Uhrig, Joachim"],["dc.contributor.author","Scheel, Dierk"],["dc.contributor.author","Lee, Justin"],["dc.date.accessioned","2019-07-09T11:44:26Z"],["dc.date.available","2019-07-09T11:44:26Z"],["dc.date.issued","2017"],["dc.identifier.doi","10.1007/s11103-017-0641-5"],["dc.identifier.pmid","28755319"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/14760"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/59012"],["dc.notes.intern","Merged from goescholar"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","A novel family of proline/serine-rich proteins, which are phospho-targets of stress-related mitogen-activated protein kinases, differentially regulates growth and pathogen defense in Arabidopsis thaliana"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1532"],["dc.bibliographiccitation.issue","12"],["dc.bibliographiccitation.journal","Cells"],["dc.bibliographiccitation.volume","8"],["dc.contributor.author","Li, Ning"],["dc.contributor.author","Uhrig, Joachim F."],["dc.contributor.author","Thurow, Corinna"],["dc.contributor.author","Huang, Li-Jun"],["dc.contributor.author","Gatz, Christiane"],["dc.date.accessioned","2020-12-10T18:46:59Z"],["dc.date.available","2020-12-10T18:46:59Z"],["dc.date.issued","2019"],["dc.description.sponsorship","the National Natural Science Foundation of China"],["dc.identifier.doi","10.3390/cells8121532"],["dc.identifier.eissn","2073-4409"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/78605"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.publisher","MDPI"],["dc.relation.eissn","2073-4409"],["dc.rights","https://creativecommons.org/licenses/by/4.0/"],["dc.title","Reconstitution of the Jasmonate Signaling Pathway in Plant Protoplasts"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","218"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms"],["dc.bibliographiccitation.lastpage","226"],["dc.bibliographiccitation.volume","1860"],["dc.contributor.author","Uhrig, Joachim F."],["dc.contributor.author","Huang, Li-Jun"],["dc.contributor.author","Barghahn, Sina"],["dc.contributor.author","Willmer, Moritz"],["dc.contributor.author","Thurow, Corinna"],["dc.contributor.author","Gatz, Christiane"],["dc.date.accessioned","2018-11-07T10:27:58Z"],["dc.date.available","2018-11-07T10:27:58Z"],["dc.date.issued","2017"],["dc.description.abstract","Glutaredoxins (GRXs) are small proteins which bind glutathione to either reduce disulfide bonds or to coordinate iron sulfur clusters. Whereas these well-established functions are associated with ubiquitously occurring GRXs that encode variants of a CPYC or a CGFS motif in the active center, land plants also possess CCxC/S-type GRXs (named ROXYs in Arabidopsis thaliana) for which the biochemical functions are yet unknown. ROXYs and CC type GRXs from rice and maize physically and genetically interact with bZIP transcription factors of the TGA family to control developmental and stress-associated processes. Here we demonstrate that ROXYs interact with transcriptional co-repressors of the TOPLESS (TPL) family which are related to Tup1 in fungi and GrouchoffLE in animals. In ROXYs, the functionally important conserved A(L/I)W(L/V) motif at the very C terminus mediates the interaction with TPL. A ternary TGA2/ROXY19/TPL complex is formed when all three proteins are co expressed in yeast. Loss-of-function evidence for the role of TPL in ROXY19-mediated repression was hampered by the redundancy of the five members of the TPL gene family and developmental defects of higher order tpl mutants. As an alternative strategy, we ectopically expressed known TPL-interacting proteins in order to out compete the amount of available TPL in transiently transformed protoplasts. Indeed, ROXY19-mediated transcriptional repression was strongly alleviated by this approach. Our data suggest a yet unrecognized function of GRXs acting as adapter proteins for the assembly of transcriptional repressor complexes on TGA-regulated target promoters. (C) 2016 Published by Elsevier B.V."],["dc.identifier.doi","10.1016/j.bbagrm.2016.11.001"],["dc.identifier.isi","000394072900005"],["dc.identifier.pmid","27838237"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/43326"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Elsevier Science Bv"],["dc.relation.issn","0006-3002"],["dc.relation.issn","1874-9399"],["dc.title","CC-type glutaredoxins recruit the transcriptional co-repressor TOPLESS to TGA-dependent target promoters in Arabidopsis thaliana"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","592"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","New Phytologist"],["dc.bibliographiccitation.lastpage","606"],["dc.bibliographiccitation.volume","203"],["dc.contributor.author","Pecher, Pascal"],["dc.contributor.author","Eschen-Lippold, Lennart"],["dc.contributor.author","Herklotz, Siska"],["dc.contributor.author","Kuhle, Katja"],["dc.contributor.author","Naumann, Kai"],["dc.contributor.author","Bethke, Gerit"],["dc.contributor.author","Uhrig, Joachim F."],["dc.contributor.author","Weyhe, Martin"],["dc.contributor.author","Scheel, Dierk"],["dc.contributor.author","Lee, Justin"],["dc.date.accessioned","2018-11-07T09:38:31Z"],["dc.date.available","2018-11-07T09:38:31Z"],["dc.date.issued","2014"],["dc.description.abstract","Mitogen-activated protein kinase (MAPK) cascades play key roles in plant immune signalling, and elucidating their regulatory functions requires the identification of the pathway-specific substrates. We used yeast two-hybrid interaction screens, in vitro kinase assays and mass spectrometry-based phosphosite mapping to study a family of MAPK substrates. Site-directed mutagenesis and promoter-reporter fusion studies were performed to evaluate the impact of substrate phosphorylation on downstream signalling. A subset of the Arabidopsis thaliana VQ-motif-containing proteins (VQPs) were phosphorylated by the MAPKs MPK3 and MPK6, and renamed MPK3/6-targeted VQPs (MVQs). When plant protoplasts (expressing these MVQs) were treated with the flagellin-derived peptide flg22, several MVQs were destabilized in vivo. The MVQs interact with specific WRKY transcription factors. Detailed analysis of a representative member of the MVQ subset, MVQ1, indicated a negative role in WRKY-mediated defence gene expression - with mutation of the VQ-motif abrogating WRKY binding and causing mis-regulation of defence gene expression. We postulate the existence of a variety of WRKY-VQP-containing transcriptional regulatory protein complexes that depend on spatio-temporal VQP and WRKY expression patterns. Defence gene transcription can be modulated by changing the composition of these complexes - in part - through MAPK-mediated VQP degradation."],["dc.identifier.doi","10.1111/nph.12817"],["dc.identifier.isi","000337639800023"],["dc.identifier.pmid","24750137"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/33079"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Wiley-blackwell"],["dc.relation.issn","1469-8137"],["dc.relation.issn","0028-646X"],["dc.title","The Arabidopsis thaliana mitogen-activated protein kinases MPK3 and MPK6 target a subclass of \"VQ-motif'-containing proteins to regulate immune responses"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]