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  1. Artikel ; Online: ZBP1 causes inflammation by inducing RIPK3-mediated necroptosis and RIPK1 kinase activity-independent apoptosis.

    Koerner, Lioba / Wachsmuth, Laurens / Kumari, Snehlata / Schwarzer, Robin / Wagner, Theresa / Jiao, Huipeng / Pasparakis, Manolis

    Cell death and differentiation

    2024  

    Abstract: Z-DNA binding protein 1 (ZBP1) has important functions in anti-viral immunity and in the regulation of inflammatory responses. ZBP1 induces necroptosis by directly engaging and activating RIPK3, however, the mechanisms by which ZBP1 induces inflammation ... ...

    Abstract Z-DNA binding protein 1 (ZBP1) has important functions in anti-viral immunity and in the regulation of inflammatory responses. ZBP1 induces necroptosis by directly engaging and activating RIPK3, however, the mechanisms by which ZBP1 induces inflammation and in particular the role of RIPK1 and the contribution of cell death-independent signaling remain elusive. Here we show that ZBP1 causes skin inflammation by inducing RIPK3-mediated necroptosis and RIPK1-caspase-8-mediated apoptosis in keratinocytes. ZBP1 induced TNFR1-independent skin inflammation in mice with epidermis-specific ablation of FADD by triggering keratinocyte necroptosis. Moreover, transgenic expression of C-terminally truncated constitutively active ZBP1 (ZBP1ca) in mouse epidermis caused skin inflammation that was only partially inhibited by abrogation of RIPK3-MLKL-dependent necroptosis and fully prevented by combined deficiency in MLKL and caspase-8. Importantly, ZBP1ca induced caspase-8-mediated skin inflammation by RHIM-dependent but kinase activity-independent RIPK1 signaling. Furthermore, ZBP1ca-induced inflammatory cytokine production in the skin was completely prevented by combined inhibition of apoptosis and necroptosis arguing against a cell death-independent pro-inflammatory function of ZBP1. Collectively, these results showed that ZBP1 induces inflammation by activating necroptosis and RIPK1 kinase activity-independent apoptosis.
    Sprache Englisch
    Erscheinungsdatum 2024-06-07
    Erscheinungsland England
    Dokumenttyp Journal Article
    ZDB-ID 1225672-9
    ISSN 1476-5403 ; 1350-9047
    ISSN (online) 1476-5403
    ISSN 1350-9047
    DOI 10.1038/s41418-024-01321-6
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  2. Buch ; Online ; Dissertation / Habilitation: Cell death and inflammation in skin homeostasis and small cell lung cancer

    Körner, Lioba Katharina [Verfasser] / Pasparakis, Manolis [Gutachter]

    2023  

    Verfasserangabe Lioba Katharina Körner ; Gutachter: Manolis Pasparakis
    Schlagwörter Naturwissenschaften ; Science
    Thema/Rubrik (Code) sg500
    Sprache Englisch
    Verlag Universitäts- und Stadtbibliothek Köln
    Erscheinungsort Köln
    Dokumenttyp Buch ; Online ; Dissertation / Habilitation
    Datenquelle Digitale Dissertationen im Internet

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  3. Artikel ; Online: NEMO- and RelA-dependent NF-κB signaling promotes small cell lung cancer.

    Koerner, Lioba / Schmiel, Marcel / Yang, Tsun-Po / Peifer, Martin / Buettner, Reinhard / Pasparakis, Manolis

    Cell death and differentiation

    2023  Band 30, Heft 4, Seite(n) 938–951

    Abstract: Small cell lung cancer (SCLC) is an aggressive type of lung cancer driven by combined loss of the tumor suppressors RB1 and TP53. SCLC is highly metastatic and despite good initial response to chemotherapy patients usually relapse, resulting in poor ... ...

    Abstract Small cell lung cancer (SCLC) is an aggressive type of lung cancer driven by combined loss of the tumor suppressors RB1 and TP53. SCLC is highly metastatic and despite good initial response to chemotherapy patients usually relapse, resulting in poor survival. Therefore, better understanding of the mechanisms driving SCLC pathogenesis is required to identify new therapeutic targets. Here we identified a critical role of the IKK/NF-κB signaling pathway in SCLC development. Using a relevant mouse model of SCLC, we found that ablation of NEMO/IKKγ, the regulatory subunit of the IKK complex that is essential for activation of canonical NF-κB signaling, strongly delayed the onset and growth of SCLC resulting in considerably prolonged survival. In addition, ablation of the main NF-κB family member p65/RelA also delayed the onset and growth of SCLC and prolonged survival, albeit to a lesser extent than NEMO. Interestingly, constitutive activation of IKK/NF-κB signaling within the tumor cells did not exacerbate the pathogenesis of SCLC, suggesting that endogenous NF-κB levels are sufficient to fully support tumor development. Moreover, TNFR1 deficiency did not affect the development of SCLC, showing that TNF signaling does not play an important role in this tumor type. Taken together, our results revealed that IKK/NF-κB signaling plays an important role in promoting SCLC, identifying the IKK/NF-κB pathway as a promising therapeutic target.
    Mesh-Begriff(e) Animals ; Mice ; I-kappa B Kinase/genetics ; I-kappa B Kinase/metabolism ; Intracellular Signaling Peptides and Proteins/metabolism ; Lung Neoplasms/genetics ; NF-kappa B/metabolism ; Signal Transduction ; Small Cell Lung Carcinoma/genetics
    Chemische Substanzen I-kappa B Kinase (EC 2.7.11.10) ; Intracellular Signaling Peptides and Proteins ; NEMO protein, mouse ; NF-kappa B ; Rela protein, mouse
    Sprache Englisch
    Erscheinungsdatum 2023-01-18
    Erscheinungsland England
    Dokumenttyp Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1225672-9
    ISSN 1476-5403 ; 1350-9047
    ISSN (online) 1476-5403
    ISSN 1350-9047
    DOI 10.1038/s41418-023-01112-5
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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    Verfügbar in ZB MED Köln/Königswinter

    Zs.A 4230: Hefte anzeigen Standort:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (2.OG)
    ab Jg. 2022: Lesesaal (EG)
    Zs.MG 80: Hefte anzeigen

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  4. Artikel ; Online: Thermosensation in Caenorhabditis elegans is linked to ubiquitin-dependent protein turnover via insulin and calcineurin signalling.

    Segref, Alexandra / Vakkayil, Kavya L / Padvitski, Tsimafei / Li, Qiaochu / Kroef, Virginia / Lormann, Jakob / Körner, Lioba / Finger, Fabian / Hoppe, Thorsten

    Nature communications

    2022  Band 13, Heft 1, Seite(n) 5874

    Abstract: Organismal physiology and survival are influenced by environmental conditions and linked to protein quality control. Proteome integrity is achieved by maintaining an intricate balance between protein folding and degradation. In Caenorhabditis elegans, ... ...

    Abstract Organismal physiology and survival are influenced by environmental conditions and linked to protein quality control. Proteome integrity is achieved by maintaining an intricate balance between protein folding and degradation. In Caenorhabditis elegans, acute heat stress determines cell non-autonomous regulation of chaperone levels. However, how the perception of environmental changes, including physiological temperature, affects protein degradation remains largely unexplored. Here, we show that loss-of-function of dyf-1 in Caenorhabditis elegans associated with dysfunctional sensory neurons leads to defects in both temperature perception and thermal adaptation of the ubiquitin/proteasome system centered on thermosensory AFD neurons. Impaired perception of moderate temperature changes worsens ubiquitin-dependent proteolysis in intestinal cells. Brain-gut communication regulating protein turnover is mediated by upregulation of the insulin-like peptide INS-5 and inhibition of the calcineurin-regulated forkhead-box transcription factor DAF-16/FOXO. Our data indicate that perception of ambient temperature and its neuronal integration is important for the control of proteome integrity in complex organisms.
    Mesh-Begriff(e) Animals ; Caenorhabditis elegans/metabolism ; Caenorhabditis elegans Proteins/metabolism ; Calcineurin/genetics ; Calcineurin/metabolism ; Forkhead Transcription Factors/genetics ; Forkhead Transcription Factors/metabolism ; Insulin/metabolism ; Proteasome Endopeptidase Complex/metabolism ; Proteolysis ; Proteome/metabolism ; Sensory Receptor Cells/metabolism ; Transcription Factors/metabolism ; Ubiquitin/metabolism
    Chemische Substanzen Caenorhabditis elegans Proteins ; Forkhead Transcription Factors ; Insulin ; Proteome ; Transcription Factors ; Ubiquitin ; Calcineurin (EC 3.1.3.16) ; Proteasome Endopeptidase Complex (EC 3.4.25.1)
    Sprache Englisch
    Erscheinungsdatum 2022-10-05
    Erscheinungsland England
    Dokumenttyp Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 2553671-0
    ISSN 2041-1723 ; 2041-1723
    ISSN (online) 2041-1723
    ISSN 2041-1723
    DOI 10.1038/s41467-022-33467-7
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  5. Artikel ; Online: Histone Purification Combined with High-Resolution Mass Spectrometry to Examine Histone Post-Translational Modifications and Histone Variants in Caenorhabditis elegans.

    Millan-Ariño, Lluís / Yuan, Zuo-Fei / Oomen, Marlies E / Brandenburg, Simone / Chernobrovkin, Alexey / Salignon, Jérôme / Körner, Lioba / Zubarev, Roman A / Garcia, Benjamin A / Riedel, Christian G

    Current protocols in protein science

    2020  Band 102, Heft 1, Seite(n) e114

    Abstract: Histones are the major proteinaceous component of chromatin in eukaryotic cells and an important part of the epigenome, affecting most DNA-related events, including transcription, DNA replication, and chromosome segregation. The properties of histones ... ...

    Abstract Histones are the major proteinaceous component of chromatin in eukaryotic cells and an important part of the epigenome, affecting most DNA-related events, including transcription, DNA replication, and chromosome segregation. The properties of histones are greatly influenced by their post-translational modifications (PTMs), over 200 of which are known today. Given this large number, researchers need sophisticated methods to study histone PTMs comprehensively. In particular, mass spectrometry (MS)-based approaches have gained popularity, allowing for the quantification of dozens of histone PTMs at once. Using these approaches, even the study of co-occurring PTMs and the discovery of novel PTMs become feasible. The success of MS-based approaches relies substantially on obtaining pure and well-preserved histones for analysis, which can be difficult depending on the source material. Caenorhabditis elegans has been a popular model organism to study the epigenome, but isolation of pure histones from these animals has been challenging. Here, we address this issue, presenting a method for efficient isolation of pure histone proteins from C. elegans at good yield. Further, we describe an MS pipeline optimized for accurate relative quantification of histone PTMs from C. elegans. We alkylate and tryptically digest the histones, analyze them by bottom-up MS, and then evaluate the resulting data by a C. elegans-adapted version of the software EpiProfile 2.0. Finally, we show the utility of this pipeline by determining differences in histone PTMs between C. elegans strains that age at different rates and thereby achieve very different lifespans. © 2020 The Authors. Basic Protocol 1: Large-scale growth and harvesting of synchronized C. elegans Basic Protocol 2: Nuclear preparation, histone extraction, and histone purification Basic Protocol 3: Bottom-up mass spectrometry analysis of histone PTMs and histone variants.
    Mesh-Begriff(e) Animals ; Caenorhabditis elegans/chemistry ; Caenorhabditis elegans/metabolism ; Caenorhabditis elegans Proteins/chemistry ; Caenorhabditis elegans Proteins/isolation & purification ; Caenorhabditis elegans Proteins/metabolism ; Histones/chemistry ; Histones/isolation & purification ; Histones/metabolism ; Protein Processing, Post-Translational ; Software ; Tandem Mass Spectrometry
    Chemische Substanzen Caenorhabditis elegans Proteins ; Histones
    Sprache Englisch
    Erscheinungsdatum 2020-09-22
    Erscheinungsland United States
    Dokumenttyp Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 2179077-2
    ISSN 1934-3663 ; 1934-3655
    ISSN (online) 1934-3663
    ISSN 1934-3655
    DOI 10.1002/cpps.114
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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