Linear ubiquitination is involved in the pathogenesis of optineurin-associated amyotrophic lateral sclerosis View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2016-08-24

AUTHORS

Seshiru Nakazawa, Daisuke Oikawa, Ryohei Ishii, Takashi Ayaki, Hirotaka Takahashi, Hiroyuki Takeda, Ryuichiro Ishitani, Kiyoko Kamei, Izumi Takeyoshi, Hideshi Kawakami, Kazuhiro Iwai, Izuho Hatada, Tatsuya Sawasaki, Hidefumi Ito, Osamu Nureki, Fuminori Tokunaga

ABSTRACT

Optineurin (OPTN) mutations cause neurodegenerative diseases, including amyotrophic lateral sclerosis (ALS) and glaucoma. Although the ALS-associated E478G mutation in the UBAN domain of OPTN reportedly abolishes its NF-κB suppressive activity, the precise molecular basis in ALS pathogenesis still remains unclear. Here we report that the OPTN-UBAN domain is crucial for NF-κB suppression. Our crystal structure analysis reveals that OPTN-UBAN binds linear ubiquitin with homology to NEMO. TNF-α-mediated NF-κB activation is enhanced in OPTN-knockout cells, through increased ubiquitination and association of TNF receptor (TNFR) complex I components. Furthermore, OPTN binds caspase 8, and OPTN deficiency accelerates TNF-α-induced apoptosis by enhancing complex II formation. Immunohistochemical analyses of motor neurons from OPTN-associated ALS patients reveal that linear ubiquitin and activated NF-κB are partially co-localized with cytoplasmic inclusions, and that activation of caspases is elevated. Taken together, OPTN regulates both NF-κB activation and apoptosis via linear ubiquitin binding, and the loss of this ability may lead to ALS. More... »

PAGES

12547

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/ncomms12547

DOI

http://dx.doi.org/10.1038/ncomms12547

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1024048012

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/27552911


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469 Laboratory of Genome Science, Biosignal Genome Resource Center, Institute for Molecular and Cellular Regulation, Gunma University, 3-39-15 Showa-machi, Maebashi, Gunma 371-8512, Japan.
470 Laboratory of Molecular Cell Biology, Institute for Molecular and Cellular Regulation, Gunma University, 3-39-15 Showa-machi, Maebashi, Gunma 371-8512, Japan.
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472 https://www.grid.ac/institutes/grid.257022.0 schema:alternateName Hiroshima University
473 schema:name Department of Epidemiology, Research Institute for Radiation Biology and Medicine, Hiroshima University, 1-2-3 Kasumi, Minami-ku, Hiroshima 734-8553, Japan.
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475 https://www.grid.ac/institutes/grid.258799.8 schema:alternateName Kyoto University
476 schema:name Department of Molecular and Cellular Physiology, Graduate School of Medicine, Kyoto University, Yoshida-konoe-cho, Sakyo-ku, Kyoto 606-8501, Japan.
477 Department of Neurology, Kyoto University Graduate School of Medicine, Sakyo-ku, Shogoin, Kyoto 606-8507, Japan.
478 Department of Neurology, Wakayama Medical University, 811-1, Kimiidera, Wakayama, Wakayama 641-8510, Japan.
479 rdf:type schema:Organization
480 https://www.grid.ac/institutes/grid.261445.0 schema:alternateName Osaka City University
481 schema:name Department of Pathobiochemistry, Graduate School of Medicine, Osaka City University, 1-4-3 Asahi-machi, Abeno-ku, Osaka 545-8585, Japan.
482 Laboratory of Molecular Cell Biology, Institute for Molecular and Cellular Regulation, Gunma University, 3-39-15 Showa-machi, Maebashi, Gunma 371-8512, Japan.
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484 https://www.grid.ac/institutes/grid.26999.3d schema:alternateName University of Tokyo
485 schema:name Department of Biological Sciences, Graduate School of Science, The University of Tokyo, 2-11-16 Yayoi, Bunkyo-ku, Tokyo 113-0032, Japan.
486 rdf:type schema:Organization
487 https://www.grid.ac/institutes/grid.412857.d schema:alternateName Wakayama Medical University
488 schema:name Department of Neurology, Wakayama Medical University, 811-1, Kimiidera, Wakayama, Wakayama 641-8510, Japan.
489 rdf:type schema:Organization
 




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