Cited by 610NF-κB Signaling PathwaysUbiquitin and proteasome pathwaysImmune Response and Inflammation

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SHARPIN is a component of the NF-κB-activating linear ubiquitin chain assembly complex

Tokunaga, Fuminori, Nakagawa, Tomoko, Nakahara, Masaki, Saeki, Yasushi, Taniguchi, Masami, Sakata, Shin-ichi, Tanaka, Keiji, Nakano, Hiroyasu, Iwai, Kazuhiro·2011·Nature

DOI 10.1038/nature09815

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Abstract

Cpdm (chronic proliferative dermatitis) mice develop chronic dermatitis and an immunodeficiency with increased serum IgM, symptoms that resemble those of patients with X-linked hyper-IgM syndrome and hypohydrotic ectodermal dysplasia (XHM-ED), which is caused by mutations in NEMO (NF-κB essential modulator; also known as IKBKG). Spontaneous null mutations in the Sharpin (SHANK-associated RH domain interacting protein in postsynaptic density) gene are responsible for the cpdm phenotype in mice. SHARPIN shows significant similarity to HOIL-1L (also known as RBCK1), a component of linear ubiquitin chain assembly complex (LUBAC), which induces NF-κB activation through conjugation of linear polyubiquitin chains to NEMO. Here, we identify SHARPIN as an additional component of LUBAC. SHARPIN-containing complexes can linearly ubiquitinate NEMO and activated NF-κB. Thus, we re-define LUBAC as a complex containing SHARPIN, HOIL-1L, and HOIP (also known as RNF31). Deletion of SHARPIN drastically reduced the amount of LUBAC, which resulted in attenuated TNF-α- and CD40-mediated activation of NF-κB in mouse embryonic fibroblasts (MEFs) or B cells from cpdm mice. Considering the pleomorphic phenotype of cpdm mice, these results confirm the predicted role of LUBAC-mediated linear polyubiquitination in NF-κB activation induced by various stimuli, and strongly suggest the involvement of LUBAC-induced NF-κB activation in various disorders.

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Authors: Tokunaga, F., Nakagawa, T., Nakahara, M., Saeki, Y., Taniguchi, M., Sakata, S.-I., Tanaka, K., Nakano, H., & Iwai, K.
Affiliations: The University of Osaka (JP)
Tokyo Metropolitan Institute of Medical Science (JP)
Juntendo University (JP)
ORCID: Tokunaga, Fuminori
Saeki, Yasushi
Tanaka, Keiji
Nakano, Hiroyasu
Venue: Nature
Publisher: Springer Science and Business Media LLC
Published: 2011-03
Volume: 471
Issue: 7340
Pages: 633-636
ISSN: 0028-0836 (ISSN-L)
1476-4687
DOI: 10.1038/nature09815
OpenAlex: W2001879129
Cited by: 609
References: 26
Citations by year: 2026: 21 · 2025: 17 · 2024: 30 · 2023: 22 · 2022: 41 · 2021: 57 · 2020: 35 · 2019: 38 · 2018: 39 · 2017: 43 · 2016: 46 · 2015: 42 · 2014: 46 · 2013: 42 · 2012: 57
FWCI: 19.25
Type: journal article
Language: en
Open access: closed
Licence: www.springer.com/tdm (tdm)
Locations: Nature (publishedVersion)
PubMed (publishedVersion)
RePEc: Research Papers in Economics (submittedVersion)
Funders: Japan Society for the Promotion of Science (23659404, 21000012, 23657075)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › NF-κB Signaling Pathways
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
Life Sciences › Immunology and Microbiology › Immunology › Immune Response and Inflammation
Keywords: SHARPIN, LUBAC, NF-κB activation, HOIL-1, HOIP, TNF signaling, CD40 ligand, ubiquitin conjugation, X-linked hyper-IgM syndrome, NEMO, immunodeficiency
MeSH terms: Animals, Carrier Proteins, Cells, Cultured, Humans, Nerve Tissue Proteins, Tumor Necrosis Factor-alpha, NF-kappa B, CD40 Ligand, Ubiquitin, Ubiquitin-Protein Ligase Complexes, Ubiquitin-Protein Ligases, Multiprotein Complexes, Intracellular Signaling Peptides and Proteins, Mice, HEK293 Cells

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SHARPIN is a component of the NF-κB-activating linear ubiquitin chain assembly complex

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