HOIL-1 ubiquitin ligase activity targets unbranched glucosaccharides and is required to prevent polyglucosan accumulation.

Autor: Kelsall IR; MRC Protein Phosphorylation and Ubiquitylation Unit, School of Life Sciences, University of Dundee, Dundee, UK., McCrory EH; MRC Protein Phosphorylation and Ubiquitylation Unit, School of Life Sciences, University of Dundee, Dundee, UK., Xu Y; Cross-Faculty NMR Centre, Department of Life Sciences, Imperial College London, London, UK., Scudamore CL; Exepathology, Exeter, UK., Nanda SK; MRC Protein Phosphorylation and Ubiquitylation Unit, School of Life Sciences, University of Dundee, Dundee, UK., Mancebo-Gamella P; MRC Protein Phosphorylation and Ubiquitylation Unit, School of Life Sciences, University of Dundee, Dundee, UK., Wood NT; MRC Protein Phosphorylation and Ubiquitylation Unit, School of Life Sciences, University of Dundee, Dundee, UK., Knebel A; MRC Protein Phosphorylation and Ubiquitylation Unit, School of Life Sciences, University of Dundee, Dundee, UK., Matthews SJ; Cross-Faculty NMR Centre, Department of Life Sciences, Imperial College London, London, UK., Cohen P; MRC Protein Phosphorylation and Ubiquitylation Unit, School of Life Sciences, University of Dundee, Dundee, UK.

Publikováno v: The EMBO journal [EMBO J] 2022 Apr 19; Vol. 41 (8), pp. e109700. Date of Electronic Publication: 2022 Mar 11.

The E3 ligase HOIL-1 catalyses ester bond formation between ubiquitin and components of the Myddosome in mammalian cells.

Autor: Kelsall IR; Medical Research Council Protein Phosphorylation and Ubiquitylation Unit, School of Life Sciences, University of Dundee, Dundee DD1 5EH, Scotland, United Kingdom., Zhang J; Medical Research Council Protein Phosphorylation and Ubiquitylation Unit, School of Life Sciences, University of Dundee, Dundee DD1 5EH, Scotland, United Kingdom., Knebel A; Medical Research Council Protein Phosphorylation and Ubiquitylation Unit, School of Life Sciences, University of Dundee, Dundee DD1 5EH, Scotland, United Kingdom., Arthur JSC; Division of Cell Signalling and Immunology, School of Life Sciences, University of Dundee, Dundee DD1 5EH, Scotland, United Kingdom., Cohen P; Medical Research Council Protein Phosphorylation and Ubiquitylation Unit, School of Life Sciences, University of Dundee, Dundee DD1 5EH, Scotland, United Kingdom; p.cohen@dundee.ac.uk.

Publikováno v: Proceedings of the National Academy of Sciences of the United States of America [Proc Natl Acad Sci U S A] 2019 Jul 02; Vol. 116 (27), pp. 13293-13298. Date of Electronic Publication: 2019 Jun 17.

Blocking an N-terminal acetylation-dependent protein interaction inhibits an E3 ligase.

Autor: Scott DC; Department of Structural Biology, St. Jude Children's Research Hospital, Memphis, Tennessee, USA.; Howard Hughes Medical Institute, St. Jude Children's Research Hospital, Memphis, Tennessee, USA., Hammill JT; Department of Chemical Biology and Therapeutics, St. Jude Children's Research Hospital, Memphis, Tennessee, USA., Min J; Department of Chemical Biology and Therapeutics, St. Jude Children's Research Hospital, Memphis, Tennessee, USA., Rhee DY; Department of Cell Biology, Harvard Medical School, Boston, Massachusetts, USA., Connelly M; Department of Chemical Biology and Therapeutics, St. Jude Children's Research Hospital, Memphis, Tennessee, USA., Sviderskiy VO; Department of Structural Biology, St. Jude Children's Research Hospital, Memphis, Tennessee, USA., Bhasin D; Department of Chemical Biology and Therapeutics, St. Jude Children's Research Hospital, Memphis, Tennessee, USA., Chen Y; Department of Chemical Biology and Therapeutics, St. Jude Children's Research Hospital, Memphis, Tennessee, USA., Ong SS; Department of Chemical Biology and Therapeutics, St. Jude Children's Research Hospital, Memphis, Tennessee, USA., Chai SC; Department of Chemical Biology and Therapeutics, St. Jude Children's Research Hospital, Memphis, Tennessee, USA., Goktug AN; Department of Chemical Biology and Therapeutics, St. Jude Children's Research Hospital, Memphis, Tennessee, USA., Huang G; Laboratory of Epithelial Cancer Biology, Memorial Sloan-Kettering Cancer Center, New York, New York, USA., Monda JK; Department of Structural Biology, St. Jude Children's Research Hospital, Memphis, Tennessee, USA., Low J; Department of Chemical Biology and Therapeutics, St. Jude Children's Research Hospital, Memphis, Tennessee, USA., Kim HS; Department of Chemical Biology and Therapeutics, St. Jude Children's Research Hospital, Memphis, Tennessee, USA., Paulo JA; Department of Cell Biology, Harvard Medical School, Boston, Massachusetts, USA., Cannon JR; Department of Cell Biology, Harvard Medical School, Boston, Massachusetts, USA., Shelat AA; Department of Chemical Biology and Therapeutics, St. Jude Children's Research Hospital, Memphis, Tennessee, USA., Chen T; Department of Chemical Biology and Therapeutics, St. Jude Children's Research Hospital, Memphis, Tennessee, USA., Kelsall IR; MRC Protein Phosphorylation and Ubiquitylation Unit, University of Dundee, Dundee, UK., Alpi AF; Department of Molecular Machines and Signaling, Max Planck Institute of Biochemistry, Martinsried, Germany., Pagala V; St. Jude Proteomics Facility, St. Jude Children's Research Hospital, Memphis, Tennessee, USA., Wang X; St. Jude Proteomics Facility, St. Jude Children's Research Hospital, Memphis, Tennessee, USA., Peng J; Department of Structural Biology, St. Jude Children's Research Hospital, Memphis, Tennessee, USA.; St. Jude Proteomics Facility, St. Jude Children's Research Hospital, Memphis, Tennessee, USA., Singh B; Laboratory of Epithelial Cancer Biology, Memorial Sloan-Kettering Cancer Center, New York, New York, USA., Harper JW; Department of Cell Biology, Harvard Medical School, Boston, Massachusetts, USA., Schulman BA; Department of Structural Biology, St. Jude Children's Research Hospital, Memphis, Tennessee, USA.; Howard Hughes Medical Institute, St. Jude Children's Research Hospital, Memphis, Tennessee, USA., Guy RK; Department of Chemical Biology and Therapeutics, St. Jude Children's Research Hospital, Memphis, Tennessee, USA.

Publikováno v: Nature chemical biology [Nat Chem Biol] 2017 Aug; Vol. 13 (8), pp. 850-857. Date of Electronic Publication: 2017 Jun 05.

IFI16 and cGAS cooperate in the activation of STING during DNA sensing in human keratinocytes.

Autor: Almine JF; Division of Cell Signalling and Immunology, School of Life Sciences, University of Dundee, Dundee DD1 5EH, UK.; Division of Biomedical and Life Sciences, Faculty of Health and Medicine, Lancaster University, Lancaster LA1 4YQ, UK., O'Hare CA; Division of Cell Signalling and Immunology, School of Life Sciences, University of Dundee, Dundee DD1 5EH, UK.; Division of Biomedical and Life Sciences, Faculty of Health and Medicine, Lancaster University, Lancaster LA1 4YQ, UK., Dunphy G; Division of Cell Signalling and Immunology, School of Life Sciences, University of Dundee, Dundee DD1 5EH, UK.; Division of Biomedical and Life Sciences, Faculty of Health and Medicine, Lancaster University, Lancaster LA1 4YQ, UK., Haga IR; The Pirbright Institute, Pirbright, Surrey GU24 0NF, UK., Naik RJ; Division of Cell Signalling and Immunology, School of Life Sciences, University of Dundee, Dundee DD1 5EH, UK., Atrih A; Fingerprints Proteomics Facility, School of Life Sciences, University of Dundee, Dundee DD1 5EH, UK., Connolly DJ; School of Biochemistry and Immunology, Trinity Biomedical Sciences Institute, Trinity College Dublin, Dublin 2, Ireland., Taylor J; Division of Cell Signalling and Immunology, School of Life Sciences, University of Dundee, Dundee DD1 5EH, UK., Kelsall IR; Division of Cell Signalling and Immunology, School of Life Sciences, University of Dundee, Dundee DD1 5EH, UK., Bowie AG; School of Biochemistry and Immunology, Trinity Biomedical Sciences Institute, Trinity College Dublin, Dublin 2, Ireland., Beard PM; The Pirbright Institute, Pirbright, Surrey GU24 0NF, UK.; The Roslin Institute and The Royal (Dick) School of Veterinary Studies, University of Edinburgh, Edinburgh EH25 9RG, UK., Unterholzner L; Division of Cell Signalling and Immunology, School of Life Sciences, University of Dundee, Dundee DD1 5EH, UK.; Division of Biomedical and Life Sciences, Faculty of Health and Medicine, Lancaster University, Lancaster LA1 4YQ, UK.

Publikováno v: Nature communications [Nat Commun] 2017 Feb 13; Vol. 8, pp. 14392. Date of Electronic Publication: 2017 Feb 13.

Lys63/Met1-hybrid ubiquitin chains are commonly formed during the activation of innate immune signalling.

Autor: Emmerich CH; MRC Protein Phosphorylation and Ubiquitylation Unit, School of Life Sciences, University of Dundee, Dundee DD1 5EH, Scotland, UK., Bakshi S; MRC Protein Phosphorylation and Ubiquitylation Unit, School of Life Sciences, University of Dundee, Dundee DD1 5EH, Scotland, UK., Kelsall IR; MRC Protein Phosphorylation and Ubiquitylation Unit, School of Life Sciences, University of Dundee, Dundee DD1 5EH, Scotland, UK., Ortiz-Guerrero J; MRC Protein Phosphorylation and Ubiquitylation Unit, School of Life Sciences, University of Dundee, Dundee DD1 5EH, Scotland, UK., Shpiro N; MRC Protein Phosphorylation and Ubiquitylation Unit, School of Life Sciences, University of Dundee, Dundee DD1 5EH, Scotland, UK., Cohen P; MRC Protein Phosphorylation and Ubiquitylation Unit, School of Life Sciences, University of Dundee, Dundee DD1 5EH, Scotland, UK. Electronic address: p.cohen@dundee.ac.uk.

Publikováno v: Biochemical and biophysical research communications [Biochem Biophys Res Commun] 2016 Jun 03; Vol. 474 (3), pp. 452-461. Date of Electronic Publication: 2016 Apr 29.