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Showing 1–18 of 18 results
Advanced filters: Author: Katrin Rittinger Clear advanced filters

  • The crystal structure of a complex between the catalytic core of the HOIP subunit of the E3 ligase LUBAC and ubiquitin is reported, yielding insight into the ubiquitin transfer reaction and explaining how HOIP is capable of synthesizing linear ubiquitin chains with high specificity.

    • Benjamin Stieglitz
    • Rohini R. Rana
    • Katrin Rittinger
    Research
    Nature
    Volume: 503, P: 422-426

  • Understanding the catalytic and regulatory mechanisms of the ubiquitin system is key to tapping into its therapeutic potential in diseases where its dysfunction is implicated. Here, the authors uncover a set of catalytically dead ‘pseudo’ ubiquitin ligases with possible regulatory roles.

    • Jane Dudley-Fraser
    • Diego Esposito
    • Katrin Rittinger
    ResearchOpen Access
    Nature Communications
    Volume: 16, P: 1-15

  • Rittinger and Walden review recent structural and functional insights to contrast and compare RBR E3 ubiquitin ligases and their regulation through autoinhibition, post-translational modifications, multimerization and protein-protein interactions.

    • Helen Walden
    • Katrin Rittinger
    Reviews
    Nature Structural & Molecular Biology
    Volume: 25, P: 440-445

  • This paper presents a label-free chemoproteomics platform using data-independent acquisition to profile covalent fragment binding across the human proteome. The platform offers high reproducibility and data completeness, identifying >400 protein-ligand interactions for probe development.

    • George S. Biggs
    • Emma E. Cawood
    • Jacob T. Bush
    ResearchOpen Access
    Nature Communications
    Volume: 16, P: 1-14

  • TRIM E3 ligases are key regulators of numerous cellular functions, yet their mechanism of action remains poorly understood. Here, the authors show that paralogous TRIM2 and TRIM3 adopt different self-association and activity profiles but interact in cells to modulate their respective activities.

    • Diego Esposito
    • Jane Dudley-Fraser
    • Katrin Rittinger
    ResearchOpen Access
    Nature Communications
    Volume: 13, P: 1-14

  • Transfer of ubiquitin onto target proteins requires controlled interplay between E2 conjugating enzymes and E3 ligases. The structure of a trapped E2~Ub/RCR E3 transfer intermediate provides novel insight into the diversity of mechanisms used to fine tune this relay.

    • Sonja Lorenz
    • Katrin Rittinger
    News & Views
    Nature Chemical Biology
    Volume: 16, P: 1158-1159

  • NS1 of influenza A virus inhibits TRIM25 activity, which is an E3 ligase important for induction of the interferon response. Here, Koliopoulos et al. present structures of TRIM25 and NS1 and show how NS1 binding interferes with substrate recognition of TRIM25.

    • Marios G. Koliopoulos
    • Mathilde Lethier
    • Katrin Rittinger
    ResearchOpen Access
    Nature Communications
    Volume: 9, P: 1-13

  • The RNA-binding ubiquitin E3 ligase TRIM25 plays a critical role in antiviral immunity. Here the authors identify key RNA-binding residues of TRIM25, link RNA binding to antiviral activity, reveal RNA structural and sequence preferences, and investigate binding to the viral genome.

    • Lucía Álvarez
    • Kevin Haubrich
    • Janosch Hennig
    ResearchOpen Access
    Nature Communications
    Volume: 15, P: 1-15

  • The ovarian tumour protease (OTU) family of deubiquitinating enzymes (DUBs) are biochemically well-characterised and of therapeutic interest, however, only a few tool compounds exist to study their cellular function and therapeutic potential. Here, the authors present a chemoproteomics fragment screening platform for identifying DUB-specific hit matter, which combines activity-based protein profiling with high-throughput optimisation to enable rapid elaboration of initial fragment hits against OTU DUBs, and identify an enantioselective chloroacetamide-based covalent fragment for OTUD7B.

    • Aini Vuorinen
    • Cassandra R. Kennedy
    • Katrin Rittinger
    ResearchOpen Access
    Communications Chemistry
    Volume: 8, P: 1-12

  • The ubiquitin conjugation system regulates the canonical NF-κB activation pathway, which mediates immune responses. Linear polyubiquitin chains—in which the C terminal glycine of ubiquitin is conjugated to the α-amino group of the amino-terminal methionine of another ubiquitin—are generated by a unique ubiquitin ligase complex called linear ubiquitin chain assembly complex (LUBAC) composed of two RING domain proteins called HOIL-1 and HOIP. This is one of three complementary studies identifying a novel component of the LUBAC complex called SHARPIN, which is recruited to receptor signalling complexes (RSCs) that form after TNF and CD40L stimulation. The LUBAC complex containing SHARPIN stimulates the formation of linear ubiquitin chains in vitro and in vivo and is required for the activation of NF-κB signalling.

    • Fumiyo Ikeda
    • Yonathan Lissanu Deribe
    • Ivan Dikic
    Research
    Nature
    Volume: 471, P: 637-641