The E3 ubiquitin ligase MIB2 enhances inflammation by degrading the deubiquitinating enzyme CYLD.


Journal

The Journal of biological chemistry
ISSN: 1083-351X
Titre abrégé: J Biol Chem
Pays: United States
ID NLM: 2985121R

Informations de publication

Date de publication:
20 09 2019
Historique:
received: 09 07 2019
pubmed: 2 8 2019
medline: 13 5 2020
entrez: 2 8 2019
Statut: ppublish

Résumé

The tumor suppressor CYLD is a deubiquitinating enzyme that suppresses polyubiquitin-dependent signaling pathways, including the proinflammatory and cell growth-promoting NF-κB pathway. Missense mutations in the

Identifiants

pubmed: 31366726
pii: S0021-9258(20)32096-2
doi: 10.1074/jbc.RA119.010119
pmc: PMC6755803
doi:

Substances chimiques

NF-kappa B 0
RELA protein, human 0
Transcription Factor RelA 0
Tumor Necrosis Factor-alpha 0
Ubiquitin 0
Polyubiquitin 120904-94-1
MIB2 protein, human EC 2.3.2.27
Ubiquitin-Protein Ligases EC 2.3.2.27
CYLD protein, human EC 3.4.19.12
CYLD protein, mouse EC 3.4.19.12
Deubiquitinating Enzyme CYLD EC 3.4.19.12
Deubiquitinating Enzymes EC 3.4.19.12
Cysteine Endopeptidases EC 3.4.22.-
Proteasome Endopeptidase Complex EC 3.4.25.1

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

14135-14148

Informations de copyright

© 2019 Uematsu et al.

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Auteurs

Atsushi Uematsu (A)

Division of Cell-Free Sciences, Proteo-Science Center (PROS), 3 Bunkyo-cho, Matsuyama, Ehime 790-8577, Japan.

Kohki Kido (K)

Division of Cell-Free Sciences, Proteo-Science Center (PROS), 3 Bunkyo-cho, Matsuyama, Ehime 790-8577, Japan.

Hirotaka Takahashi (H)

Division of Cell-Free Sciences, Proteo-Science Center (PROS), 3 Bunkyo-cho, Matsuyama, Ehime 790-8577, Japan.

Chikako Takahashi (C)

Division of Cell-Free Sciences, Proteo-Science Center (PROS), 3 Bunkyo-cho, Matsuyama, Ehime 790-8577, Japan.

Yuta Yanagihara (Y)

Division of Integrative Pathophysiology, PROS, 3 Bunkyo-cho, Matsuyama, Ehime 790-8577, Japan.

Noritaka Saeki (N)

Division of Integrative Pathophysiology, PROS, 3 Bunkyo-cho, Matsuyama, Ehime 790-8577, Japan.

Shuhei Yoshida (S)

Division of Integrative Pathophysiology, PROS, 3 Bunkyo-cho, Matsuyama, Ehime 790-8577, Japan.

Masashi Maekawa (M)

Division of Cell Growth and Tumor Regulation, PROS, 3 Bunkyo-cho, Matsuyama, Ehime 790-8577.
Department of Biochemistry and Molecular Genetics, Ehime University Graduate School of Medicine, Shitsukawa, Toon, Ehime 791-0295, Japan.

Mamoru Honda (M)

Pharmaceuticals and Life Sciences Division, Shimadzu Techno-Research, Inc., Nishinokyo-Shimoaicho, Nakagyo-ku, Kyoto 604-8436, Japan.

Tsutomu Kai (T)

Pharmaceuticals and Life Sciences Division, Shimadzu Techno-Research, Inc., Nishinokyo-Shimoaicho, Nakagyo-ku, Kyoto 604-8436, Japan.

Kouhei Shimizu (K)

Division of Cell-Free Sciences, Proteo-Science Center (PROS), 3 Bunkyo-cho, Matsuyama, Ehime 790-8577, Japan.

Shigeki Higashiyama (S)

Division of Cell Growth and Tumor Regulation, PROS, 3 Bunkyo-cho, Matsuyama, Ehime 790-8577.
Department of Biochemistry and Molecular Genetics, Ehime University Graduate School of Medicine, Shitsukawa, Toon, Ehime 791-0295, Japan.

Yuuki Imai (Y)

Division of Integrative Pathophysiology, PROS, 3 Bunkyo-cho, Matsuyama, Ehime 790-8577, Japan.

Fuminori Tokunaga (F)

Department of Pathobiochemistry, Graduate School of Medicine, Osaka City University, 1-4-3 Asahi-machi, Abeno-ku, Osaka 545-8585, Japan.

Tatsuya Sawasaki (T)

Division of Cell-Free Sciences, Proteo-Science Center (PROS), 3 Bunkyo-cho, Matsuyama, Ehime 790-8577, Japan sawasaki@ehime-u.ac.jp.

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Classifications MeSH