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| 001 | 140707 | ||
| 005 | 20240619102513.0 | ||
| 024 | 7 | _ | |a 10.15252/embj.2018100730 |2 doi |
| 024 | 7 | _ | |a pmid:30886048 |2 pmid |
| 024 | 7 | _ | |a pmc:PMC6484417 |2 pmc |
| 024 | 7 | _ | |a 0261-4189 |2 ISSN |
| 024 | 7 | _ | |a 1460-2075 |2 ISSN |
| 024 | 7 | _ | |a altmetric:57267821 |2 altmetric |
| 037 | _ | _ | |a DZNE-2020-07029 |
| 041 | _ | _ | |a English |
| 082 | _ | _ | |a 570 |
| 100 | 1 | _ | |a van Well, Eva M |b 0 |
| 245 | _ | _ | |a A protein quality control pathway regulated by linear ubiquitination. |
| 260 | _ | _ | |a Hoboken, NJ [u.a.] |c 2019 |b Wiley |
| 264 | _ | 1 | |3 online |2 Crossref |b EMBO |c 2019-03-18 |
| 264 | _ | 1 | |3 print |2 Crossref |b EMBO |c 2019-05-02 |
| 336 | 7 | _ | |a article |2 DRIVER |
| 336 | 7 | _ | |a Output Types/Journal article |2 DataCite |
| 336 | 7 | _ | |a Journal Article |b journal |m journal |0 PUB:(DE-HGF)16 |s 1718785470_8364 |2 PUB:(DE-HGF) |
| 336 | 7 | _ | |a ARTICLE |2 BibTeX |
| 336 | 7 | _ | |a JOURNAL_ARTICLE |2 ORCID |
| 336 | 7 | _ | |a Journal Article |0 0 |2 EndNote |
| 520 | _ | _ | |a Neurodegenerative diseases are characterized by the accumulation of misfolded proteins in the brain. Insights into protein quality control mechanisms to prevent neuronal dysfunction and cell death are crucial in developing causal therapies. Here, we report that various disease-associated protein aggregates are modified by the linear ubiquitin chain assembly complex (LUBAC). HOIP, the catalytic component of LUBAC, is recruited to misfolded Huntingtin in a p97/VCP-dependent manner, resulting in the assembly of linear polyubiquitin. As a consequence, the interactive surface of misfolded Huntingtin species is shielded from unwanted interactions, for example with the low complexity sequence domain-containing transcription factor Sp1, and proteasomal degradation of misfolded Huntingtin is facilitated. Notably, all three core LUBAC components are transcriptionally regulated by Sp1, linking defective LUBAC expression to Huntington's disease. In support of a protective activity of linear ubiquitination, silencing of OTULIN, a deubiquitinase with unique specificity for linear polyubiquitin, decreases proteotoxicity, whereas silencing of HOIP has the opposite effect. These findings identify linear ubiquitination as a protein quality control mechanism and hence a novel target for disease-modifying strategies in proteinopathies. |
| 536 | _ | _ | |a 342 - Disease Mechanisms and Model Systems (POF3-342) |0 G:(DE-HGF)POF3-342 |c POF3-342 |f POF III |x 0 |
| 536 | _ | _ | |a 344 - Clinical and Health Care Research (POF3-344) |0 G:(DE-HGF)POF3-344 |c POF3-344 |f POF III |x 1 |
| 536 | _ | _ | |a 341 - Molecular Signaling (POF3-341) |0 G:(DE-HGF)POF3-341 |c POF3-341 |f POF III |x 2 |
| 542 | _ | _ | |i 2019-03-18 |2 Crossref |u http://onlinelibrary.wiley.com/termsAndConditions#vor |
| 542 | _ | _ | |i 2019-03-18 |2 Crossref |u http://doi.wiley.com/10.1002/tdm_license_1.1 |
| 588 | _ | _ | |a Dataset connected to CrossRef, PubMed, |
| 650 | _ | 7 | |a HTT protein, human |2 NLM Chemicals |
| 650 | _ | 7 | |a Huntingtin Protein |2 NLM Chemicals |
| 650 | _ | 7 | |a NF-kappa B |2 NLM Chemicals |
| 650 | _ | 7 | |a Sp1 Transcription Factor |2 NLM Chemicals |
| 650 | _ | 7 | |a Sp1 protein, human |2 NLM Chemicals |
| 650 | _ | 7 | |a Polyubiquitin |0 120904-94-1 |2 NLM Chemicals |
| 650 | _ | 7 | |a Valosin Containing Protein |0 EC 3.6.4.6 |2 NLM Chemicals |
| 650 | _ | 2 | |a Adult |2 MeSH |
| 650 | _ | 2 | |a Aged |2 MeSH |
| 650 | _ | 2 | |a Animals |2 MeSH |
| 650 | _ | 2 | |a Brain: metabolism |2 MeSH |
| 650 | _ | 2 | |a Brain: pathology |2 MeSH |
| 650 | _ | 2 | |a Case-Control Studies |2 MeSH |
| 650 | _ | 2 | |a Cells, Cultured |2 MeSH |
| 650 | _ | 2 | |a Embryo, Mammalian: cytology |2 MeSH |
| 650 | _ | 2 | |a Embryo, Mammalian: metabolism |2 MeSH |
| 650 | _ | 2 | |a Female |2 MeSH |
| 650 | _ | 2 | |a Fibroblasts: cytology |2 MeSH |
| 650 | _ | 2 | |a Fibroblasts: metabolism |2 MeSH |
| 650 | _ | 2 | |a Humans |2 MeSH |
| 650 | _ | 2 | |a Huntingtin Protein: genetics |2 MeSH |
| 650 | _ | 2 | |a Huntingtin Protein: metabolism |2 MeSH |
| 650 | _ | 2 | |a Huntington Disease: genetics |2 MeSH |
| 650 | _ | 2 | |a Huntington Disease: metabolism |2 MeSH |
| 650 | _ | 2 | |a Huntington Disease: pathology |2 MeSH |
| 650 | _ | 2 | |a Male |2 MeSH |
| 650 | _ | 2 | |a Mice |2 MeSH |
| 650 | _ | 2 | |a Mice, Knockout |2 MeSH |
| 650 | _ | 2 | |a Middle Aged |2 MeSH |
| 650 | _ | 2 | |a NF-kappa B: genetics |2 MeSH |
| 650 | _ | 2 | |a NF-kappa B: metabolism |2 MeSH |
| 650 | _ | 2 | |a Neurons: metabolism |2 MeSH |
| 650 | _ | 2 | |a Neurons: pathology |2 MeSH |
| 650 | _ | 2 | |a Polyubiquitin: metabolism |2 MeSH |
| 650 | _ | 2 | |a Protein Binding |2 MeSH |
| 650 | _ | 2 | |a Protein Interaction Domains and Motifs |2 MeSH |
| 650 | _ | 2 | |a Protein Processing, Post-Translational |2 MeSH |
| 650 | _ | 2 | |a Signal Transduction |2 MeSH |
| 650 | _ | 2 | |a Sp1 Transcription Factor: genetics |2 MeSH |
| 650 | _ | 2 | |a Sp1 Transcription Factor: metabolism |2 MeSH |
| 650 | _ | 2 | |a Ubiquitination |2 MeSH |
| 650 | _ | 2 | |a Valosin Containing Protein: genetics |2 MeSH |
| 650 | _ | 2 | |a Valosin Containing Protein: metabolism |2 MeSH |
| 700 | 1 | _ | |a Bader, Verian |b 1 |
| 700 | 1 | _ | |a Patra, Maria |b 2 |
| 700 | 1 | _ | |a Sánchez-Vicente, Ana |b 3 |
| 700 | 1 | _ | |a Meschede, Jens |b 4 |
| 700 | 1 | _ | |a Furthmann, Nikolas |b 5 |
| 700 | 1 | _ | |a Schnack, Cathrin |b 6 |
| 700 | 1 | _ | |a Blusch, Alina |b 7 |
| 700 | 1 | _ | |a Longworth, Joseph |b 8 |
| 700 | 1 | _ | |a Petrasch-Parwez, Elisabeth |b 9 |
| 700 | 1 | _ | |a Mori, Kohji |b 10 |
| 700 | 1 | _ | |a Arzberger, Thomas |0 P:(DE-2719)2811333 |b 11 |u dzne |
| 700 | 1 | _ | |a Trümbach, Dietrich |0 P:(DE-HGF)0 |b 12 |
| 700 | 1 | _ | |a Angersbach, Lena |b 13 |
| 700 | 1 | _ | |a Showkat, Cathrin |b 14 |
| 700 | 1 | _ | |a Sehr, Dominik A |b 15 |
| 700 | 1 | _ | |a Berlemann, Lena A |b 16 |
| 700 | 1 | _ | |a Goldmann, Petra |b 17 |
| 700 | 1 | _ | |a Clement, Albrecht M |b 18 |
| 700 | 1 | _ | |a Behl, Christian |b 19 |
| 700 | 1 | _ | |a Woerner, Andreas C |b 20 |
| 700 | 1 | _ | |a Saft, Carsten |b 21 |
| 700 | 1 | _ | |a Wurst, Wolfgang |0 P:(DE-2719)2000028 |b 22 |u dzne |
| 700 | 1 | _ | |a Haass, Christian |0 P:(DE-2719)2202037 |b 23 |u dzne |
| 700 | 1 | _ | |a Ellrichmann, Gisa |b 24 |
| 700 | 1 | _ | |a Gold, Ralf |b 25 |
| 700 | 1 | _ | |a Dittmar, Gunnar |b 26 |
| 700 | 1 | _ | |a Hipp, Mark S |b 27 |
| 700 | 1 | _ | |a Hartl, F Ulrich |b 28 |
| 700 | 1 | _ | |a Tatzelt, Jörg |0 P:(DE-HGF)0 |b 29 |
| 700 | 1 | _ | |a Winklhofer, Konstanze F |0 P:(DE-2719)9000369 |b 30 |e Last author |u dzne |
| 773 | 1 | 8 | |a 10.15252/embj.2018100730 |b : EMBO, 2019-03-18 |n 9 |3 journal-article |2 Crossref |t The EMBO Journal |v 38 |y 2019 |x 0261-4189 |
| 773 | _ | _ | |a 10.15252/embj.2018100730 |g Vol. 38, no. 9 |0 PERI:(DE-600)1467419-1 |n 9 |q 38:9 |p e100730 |t The EMBO journal |v 38 |y 2019 |x 0261-4189 |
| 856 | 7 | _ | |2 Pubmed Central |u http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6484417 |
| 856 | 4 | _ | |u https://pub.dzne.de/record/140707/files/DZNE-2020-07029_Restricted.pdf |
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| 910 | 1 | _ | |a Deutsches Zentrum für Neurodegenerative Erkrankungen |0 I:(DE-588)1065079516 |k DZNE |b 11 |6 P:(DE-2719)2811333 |
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| 913 | 1 | _ | |a DE-HGF |b Gesundheit |l Erkrankungen des Nervensystems |1 G:(DE-HGF)POF3-340 |0 G:(DE-HGF)POF3-342 |3 G:(DE-HGF)POF3 |2 G:(DE-HGF)POF3-300 |4 G:(DE-HGF)POF |v Disease Mechanisms and Model Systems |x 0 |
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| 913 | 1 | _ | |a DE-HGF |b Gesundheit |l Erkrankungen des Nervensystems |1 G:(DE-HGF)POF3-340 |0 G:(DE-HGF)POF3-341 |3 G:(DE-HGF)POF3 |2 G:(DE-HGF)POF3-300 |4 G:(DE-HGF)POF |v Molecular Signaling |x 2 |
| 914 | 1 | _ | |y 2019 |
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| 920 | 1 | _ | |0 I:(DE-2719)1111016 |k AG Levin |l Clinical Neurodegeneration |x 0 |
| 920 | 1 | _ | |0 I:(DE-2719)1140001 |k AG Wurst |l Genome Engineering |x 1 |
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