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

The DOI matches its Crossref record; 26 of the 26 references it cites were found in a registry or an index.

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

Open this paper in CoChat — free account

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.

Integrity signals

Registry

Crossref · 10.1038/nature09815

Cites

26 of 26 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

This paper’s full text isn’t openly available, so its claims and self-check weren’t run. The registry and citation checks still apply.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Shared Principles in NF-κB Signaling
Hayden, M. S., & Ghosh, S. (2008) · Cell · doi:10.1016/j.cell.2008.01.020 · Cited by 4,954
Nuclear factor-κB in cancer development and progression
Karin, M. (2006) · Nature · doi:10.1038/nature04870 · Cited by 3,519
Regulation and Function of NF-κB Transcription Factors in the Immune System
Vallabhapurapu, S., & Karin, M. (2009) · Annual Review of Immunology · doi:10.1146/annurev.immunol.021908.132641 · Cited by 2,635
Complementation Cloning of NEMO, a Component of the IκB Kinase Complex Essential for NF-κB Activation
Yamaoka, S., Courtois, G., Chable-Bessia, C., Whiteside, S. T., Weil, R., Agou, F., Kirk, H., Kay, R. J., & Israël, A. (1998) · Cell · doi:10.1016/s0092-8674(00)81466-x · Cited by 1,077
Involvement of linear polyubiquitylation of NEMO in NF-κB activation
Tokunaga, F., Sakata, S., Saeki, Y., Satomi, Y., Kirisako, T., Kamei, K., Nakagawa, T., Kato, M., Murata, S., Yamaoka, S., et al. (2009) · Nature Cell Biology · doi:10.1038/ncb1821 · Cited by 960
Self-citation
A ubiquitin ligase complex assembles linear polyubiquitin chains
Kirisako, T., Kamei, K., Murata, S., Kato, M., Fukumoto, H., Kanie, M., Sano, S., Tokunaga, F., Tanaka, K., & Iwaï, K. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601360 · Cited by 803
Self-citation
Recruitment of the Linear Ubiquitin Chain Assembly Complex Stabilizes the TNF-R1 Signaling Complex and Is Required for TNF-Mediated Gene Induction
Haas, T. L., Emmerich, C. H., Gerlach, B., Schmukle, A. C., Cordier, S. M., Rieser, E., Feltham, R., Vince, J. E., Warnken, U. H., Wenger, T., et al. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.10.013 · Cited by 797
Ubiquitylation in innate and adaptive immunity
Bhoj, V. G., & Chen, Z. J. (2009) · Nature · doi:10.1038/nature07959 · Cited by 632
Distinct Roles in Lymphoid Organogenesis for Lymphotoxins α and β Revealed in Lymphotoxin β–Deficient Mice
Koni, P. A., Sacca, R. E., Lawton, P., Browning, J. L., Ruddle, N. H., & Flavell, R. A. (1997) · Immunity · doi:10.1016/s1074-7613(00)80292-7 · Cited by 589
A novel X-linked disorder of immune deficiency and hypohidrotic ectodermal dysplasia is allelic to incontinentia pigmenti and due to mutations in IKK-gamma (NEMO)
Zonana, J., Elder, M. E., Schneider, L. C., Orlow, S. J., Moss, C., Golabi, M., Shapira, S. K., Farndon, P. A., Wara, D. W., Emmal, S. A., et al. (2000) · The American Journal of Human Genetics · doi:10.1086/316914 · Cited by 521

Flagged first, then by citations

Show all 26 references

Sorted by citations

Items 301–400 of 610

Regulation of Met1‐linked polyubiquitin signalling by the deubiquitinase OTULIN
Elliott, P. R., & Komander, D. (2015) · FEBS Journal · doi:10.1111/febs.13547 · Cited by 38
Determination of the pKa of the N-terminal amino group of ubiquitin by NMR
Oregioni, A., Stieglitz, B., Kelly, G. P., Rittinger, K., & Frenkiel, T. A. (2017) · Scientific Reports · doi:10.1038/srep43748 · Cited by 38
SHARPIN stabilizes estrogen receptor α and promotes breast cancer cell proliferation
Zhuang, T., Yu, S., Zhang, L., Yang, H., Li, X., Hou, Y., Liu, Z., Shi, Y., Wang, W., Yu, N. H., et al. (2017) · Oncotarget · doi:10.18632/oncotarget.20368 · Cited by 36
Non-proteolytic ubiquitination of OTULIN regulates NF-κB signaling pathway
Zhao, M., Song, K., Hao, W., Wang, L., Patil, G., Li, Q., Xu, L., Hua, F., Fu, B., Schwamborn, J. C., et al. (2019) · Journal of Molecular Cell Biology · doi:10.1093/jmcb/mjz081 · Cited by 34
Role of Extrinsic Apoptotic Signaling Pathway during Definitive Erythropoiesis in Normal Patients and in Patients with β-Thalassemia
Raducka-Jaszul, O., Bogusławska, D. M., Jędruchniewicz, N., & Sikorski, A. F. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21093325 · Cited by 37
Shikonin promotes ubiquitination and degradation of cIAP1/2-mediated apoptosis and necrosis in triple negative breast cancer cells
Wang, A., Liu, J., Yang, Y., Chen, Z., Gao, C., Wang, Z., Fu, C., Zou, L., & Wang, S. (2021) · Chinese Medicine · doi:10.1186/s13020-021-00426-1 · Cited by 35
RIP1 post-translational modifications
Varfolomeev, E., & Vucic, D. (2022) · Biochemical Journal · doi:10.1042/bcj20210725 · Cited by 36
HOIL-1L Interacting Protein (HOIP) Is Essential for CD40 Signaling
Hostager, B. S., Kashiwada, M., Colgan, J. D., & Rothman, P. B. (2011) · PLoS ONE · doi:10.1371/journal.pone.0023061 · Cited by 35
High-Throughput Screening for Linear Ubiquitin Chain Assembly Complex (LUBAC) Selective Inhibitors Using Homogenous Time-Resolved Fluorescence (HTRF)-Based Assay System
Katsuya, K., Hori, Y., Oikawa, D., Yamamoto, T., Umetani, K., Urashima, T., Kinoshita, T., Ayukawa, K., Tokunaga, F., & Tamaru, M. (2018) · SLAS DISCOVERY · doi:10.1177/2472555218793066 · Cited by 34
Self-citation
SHARPIN at the nexus of integrin, immune, and inflammatory signaling in human platelets
Kasirer‐Friede, A., Tjahjono, W., Eto, K., & Shattil, S. J. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1819156116 · Cited by 35
Systematic analysis of the IL‐17 receptor signalosome reveals a robust regulatory feedback loop
Draberova, H., Janusova, S., Knizkova, D., Šemberová, T., Přibíková, M., Ujevic, A., Harant, K., Knápková, S., Hrdinka, M., Fanfani, V., et al. (2020) · The EMBO Journal · doi:10.15252/embj.2019104202 · Cited by 35
Unanchored Ubiquitin Chains, Revisited
Blount, J. R., Johnson, S. L., & Todi, S. V. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.582361 · Cited by 36
Compound heterozygous variants in OTULIN are associated with fulminant atypical late‐onset ORAS
Zinngrebe, J., Moepps, B., Monecke, T., Gierschik, P., Schlichtig, F., Barth, T. F. E., Strauß, G., Boldrin, E., Posovszky, C., Schulz, A., et al. (2022) · EMBO Molecular Medicine · doi:10.15252/emmm.202114901 · Cited by 36
Microbial-induced immunomodulation by targeting the NF-κB system
Neish, A. S., & Naumann, M. (2011) · Trends in Microbiology · doi:10.1016/j.tim.2011.08.004 · Cited by 33
Elevation of SIPL1 (SHARPIN) increases breast cancer risk
De Melo, J., & Tang, D. (2015) · PLOS ONE · doi:10.1371/journal.pone.0127546 · Cited by 33
Noncovalent Ubiquitin Interactions Regulate the Catalytic Activity of Ubiquitin Writers
Wright, J. D., Mace, P. D., & Day, C. L. (2016) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2016.08.003 · Cited by 33
Innate immune adaptor MyD88 deficiency prevents skin inflammation in SHARPIN-deficient mice
Sharma, B. R., Karki, R., Lee, E., Zhu, Q., Gurung, P., & Kanneganti, T. (2018) · Cell Death and Differentiation · doi:10.1038/s41418-018-0159-7 · Cited by 33
The regulation of necroptosis by ubiquitylation
Chen, Y., Ren, W., Wang, Q., He, Y., Ma, D., & Cai, Z. (2022) · APOPTOSIS · doi:10.1007/s10495-022-01755-8 · Cited by 32
SHARPIN Is Essential for Cytokine Production, NF-κB Signaling, and Induction of Th1 Differentiation by Dendritic Cells
Wang, Z., Sokolovska, A., Seymour, R. E., Sundberg, J. P., & HogenEsch, H. (2012) · PLoS ONE · doi:10.1371/journal.pone.0031809 · Cited by 33
Sharpin promotes hepatocellular carcinoma progression via transactivation of Versican expression
Tanaka, Y., Tateishi, K., Nakatsuka, T., Kudo, Y., Takahashi, R., Miyabayashi, K., Yamamoto, K., Asaoka, Y., Ijichi, H., Tateishi, R., et al. (2016) · Oncogenesis · doi:10.1038/oncsis.2016.76 · Cited by 34
Dominant negative OTULIN-related autoinflammatory syndrome
Davidson, S., Shibata, Y., Collard, S., Zheng, H., Kong, K., Sun, J., Laohamonthonkul, P., Cerra, A., Kratina, T., CIRCA, et al. (2024) · The Journal of Experimental Medicine · doi:10.1084/jem.20222171 · Cited by 31
LUBAC Formation Is Impaired in the Livers of Mice with MCD‐Dependent Nonalcoholic Steatohepatitis
Matsunaga, Y., Nakatsu, Y., Fukushima, T., Okubo, H., Iwashita, M., Sakoda, H., Fujishiro, M., Yamamotoya, T., Kushiyama, A., Takahashi, S., et al. (2015) · Mediators of Inflammation · doi:10.1155/2015/125380 · Cited by 32
Self-citation
Linear polyubiquitin chains
Iwaï, K. (2011) · Cell Cycle · doi:10.4161/cc.10.18.17437 · Cited by 32
OTULIN allies with LUBAC to govern angiogenesis by editing ALK1 linear polyubiquitin
Fu, Y., Wang, H., Dai, H., Zhu, Q., Cui, C., Sun, X., Li, Y., Deng, Z., Zhou, X., Ge, Y., et al. (2021) · Molecular Cell · doi:10.1016/j.molcel.2021.05.031 · Cited by 33
Innovative Medicine
Nakao, K., Minato, N., & Üemoto, S. (2015) · Springer eBooks · doi:10.1007/978-4-431-55651-0 · Cited by 34
Structure of a compact conformation of linear diubiquitin
Rohaim, A., Kawasaki, M., Kato, R., Đikić, I., & Wakatsuki, S. (2012) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444911051195 · Cited by 31
Sweet modification and regulation of death receptor signalling pathway
Moriwaki, K., Chan, F. K.-M., & Miyoshi, E. (2021) · The Journal of Biochemistry · doi:10.1093/jb/mvab034 · Cited by 32
Epithelial Cell Death and Inflammation in Skin
Kumari, S., & Pasparakis, M. (2015) · Current topics in microbiology and immunology · doi:10.1007/82_2015_466 · Cited by 33
The seventh zinc finger motif of A20 is required for the suppression of TNF‐α‐induced apoptosis
Yamaguchi, N., & Yamaguchi, N. (2015) · FEBS Letters · doi:10.1016/j.febslet.2015.04.022 · Cited by 33
Distinct role of IL-1β in instigating disease in Sharpincpdm mice
Gurung, P., Sharma, B. R., & Kanneganti, T. (2016) · Scientific Reports · doi:10.1038/srep36634 · Cited by 31
Genomics, Biology, and Human Illness
Oda, H., & Kastner, D. L. (2017) · Rheumatic Disease Clinics of North America · doi:10.1016/j.rdc.2017.04.011 · Cited by 29
Targeting RIP Kinases in Chronic Inflammatory Disease
Speir, M., Djajawi, T. M., Conos, S. A., Tye, H., & Lawlor, K. E. (2021) · Biomolecules · doi:10.3390/biom11050646 · Cited by 30
HOIP limits anti-tumor immunity by protecting against combined TNF and IFN-gamma-induced apoptosis
Freeman, A. J., Vervoort, S. J., Michie, J., Ramsbottom, K. M., Silke, J., Kearney, C. J., & Oliaro, J. (2021) · EMBO Reports · doi:10.15252/embr.202153391 · Cited by 31
Structural Analysis of SHARPIN, a Subunit of a Large Multi-protein E3 Ubiquitin Ligase, Reveals a Novel Dimerization Function for the Pleckstrin Homology Superfold
Stieglitz, B., Haire, L. F., Đikić, I., & Rittinger, K. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.359547 · Cited by 32
An Essential Role for SHARPIN in the Regulation of Caspase 1 Activity in Sepsis
Nastase, M.-V., Zeng-Brouwers, J., Frey, H., Hsieh, L. T.-H., Poluzzi, C., Beckmann, J., Schroeder, N., Pfeilschifter, J. M., López-Mosqueda, J., Mersmann, J., et al. (2016) · American Journal Of Pathology · doi:10.1016/j.ajpath.2015.12.026 · Cited by 30
Transcriptomic Analysis of Stem Cells Treated with Moringin or Cannabidiol: Analogies and Differences in Inflammation Pathways
Chiricosta, L., Silvestro, S., Pizzicannella, J., Diomede, F., Bramanti, P., Trubiani, O., & Mazzon, E. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20236039 · Cited by 30
Immune Response in H. pylori-Associated Gastritis and Gastric Cancer
Niu, Q., Zhu, J., Yu, X., Feng, T., Ji, H., Li, Y., Zhang, W., & Hu, B. (2020) · Gastroenterology Research and Practice · doi:10.1155/2020/9342563 · Cited by 29
LUBAC controls chromosome alignment by targeting CENP-E to attached kinetochores
Wu, M., Chang, Y. Z., Hu, H., Mu, R., Zhang, Y., Qin, X.-H., Duan, X., Li, W., Tu, H.-Q., Zhang, W., et al. (2019) · Nature Communications · doi:10.1038/s41467-018-08043-7 · Cited by 31
A novel gammaretroviral shuttle vector insertional mutagenesis screen identifies SHARPIN as a breast cancer metastasis gene and prognostic biomarker
Bii, V. M., Rae, D. T., & Trobridge, G. D. (2015) · Oncotarget · doi:10.18632/oncotarget.6232 · Cited by 28
Sharpin Contributes to TNFα Dependent NFκB Activation and Anti-Apoptotic Signalling in Hepatocytes
Sieber, S., Lange, N., Kollmorgen, G., Erhardt, A., Quaas, A., Gontarewicz, A., Sass, G., Tiegs, G., & Kreienkamp, H. (2012) · PLoS ONE · doi:10.1371/journal.pone.0029993 · Cited by 28
Structure and Specificity of the Bacterial Cysteine Methyltransferase Effector NleE Suggests a Novel Substrate in Human DNA Repair Pathway
Yao, Q., Zhang, L., Wan, X., Chen, J., Hu, L., Ding, X., Li, L., Karar, J., Peng, H., Chen, S., et al. (2014) · PLoS Pathogens · doi:10.1371/journal.ppat.1004522 · Cited by 29
Modulation of autoimmune pathogenesis by T cell-triggered inflammatory cell death
Sasaki, K., Himeno, A., Nakagawa, T., Sasaki, Y., Kiyonari, H., & Iwaï, K. (2019) · Nature Communications · doi:10.1038/s41467-019-11858-7 · Cited by 33
Self-citation
Atypical ubiquitin-binding protein SHARPIN promotes breast cancer progression
Tian, Z., Tang, J., Yang, Q., Li, X., Zhu, J., & Wu, G. (2019) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2019.109414 · Cited by 27
Differential Involvement of the Npl4 Zinc Finger Domains of SHARPIN and HOIL-1L in Linear Ubiquitin Chain Assembly Complex-Mediated Cell Death Protection
Shimizu, S., Fujita, H., Sasaki, Y., Tsuruyama, T., Fukuda, K., & Iwaï, K. (2016) · Molecular and Cellular Biology · doi:10.1128/mcb.01049-15 · Cited by 28
Discovery of linear ubiquitination, a crucial regulator for immune signaling and cell death
Iwaï, K. (2020) · FEBS Journal · doi:10.1111/febs.15471 · Cited by 30
Linear ubiquitination at damaged lysosomes induces local NFKB activation and controls cell survival
Zein, L., Dietrich, M., Balta, D., Bader, V., Scheuer, C., Zellner, S., Weinelt, N., Vandrey, J., Mari, M. C., Behrends, C., et al. (2025) · Autophagy · doi:10.1080/15548627.2024.2443945 · Cited by 31
Biochemistry, Pathophysiology, and Regulation of Linear Ubiquitination: Intricate Regulation by Coordinated Functions of the Associated Ligase and Deubiquitinase
Fuseya, Y., & Iwaï, K. (2021) · Cells · doi:10.3390/cells10102706 · Cited by 28
De novo mapping of α-helix recognition sites on protein surfaces using unbiased libraries
Li, K., Tokareva, O. S., Thomson, T. M., Wahl, S. C. T., Travaline, T. L., Ramirez, J. D., Choudary, S. K., Agarwal, S., Walkup, W. G., Olsen, T. J., et al. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2210435119 · Cited by 27
Cloaked in ubiquitin, a killer hides in plain sight: the molecular regulation of RIPK 1
Justus, S. J., & Ting, A. T. (2015) · Immunological Reviews · doi:10.1111/imr.12304 · Cited by 27
Protein ubiquitination in lymphoid malignancies
Yang, Y., & Staudt, L. M. (2014) · Immunological Reviews · doi:10.1111/imr.12247 · Cited by 27
Cooperative Immune Suppression by Escherichia coli and Shigella Effector Proteins
de Jong, M. F., & Alto, N. M. (2018) · Infection and Immunity · doi:10.1128/iai.00560-17 · Cited by 27
Synergistic activation of NF-κB by TNFAIP3 (A20) reduction and UBE2L3 (UBCH7) augment that synergistically elevate lupus risk
Kim, T., Bae, S., & Kang, C. (2020) · Arthritis Research & Therapy · doi:10.1186/s13075-020-02181-4 · Cited by 27
Glycogen synthase downregulation rescues the amylopectinosis of murine RBCK1 deficiency
Nitschke, S., Sullivan, M. A., Mitra, S., Marchioni, C. R., Lee, J. P. Y., Smith, B. H., Ahonen, S., Wu, J., Chown, E. E., Wang, P., et al. (2022) · Brain · doi:10.1093/brain/awac017 · Cited by 25
Kaposi’s Sarcoma Associated Herpesvirus Encoded Viral FLICE Inhibitory Protein K13 Activates NF-κB Pathway Independent of TRAF6, TAK1 and LUBAC
Matta, H., Ramakrishnan, G., Graham, C., Tolani, B., Khanna, A., Yi, H., Suo, Y., & Chaudhary, P. M. (2012) · PLoS ONE · doi:10.1371/journal.pone.0036601 · Cited by 26
Gene Expression Profile of Bombyx mori Hemocyte under the Stress of Destruxin A
Gong, L., Chen, X., Liu, C., Jin, F., & Hu, Q. (2014) · PLoS ONE · doi:10.1371/journal.pone.0096170 · Cited by 26
The parkin-coregulated gene product PACRG promotes TNF signaling by stabilizing LUBAC
Meschede, J., Šadič, M., Furthmann, N., Miedema, T., Sehr, D. A., Müller-Rischart, A. K., Bader, V., Berlemann, L. A., Pilsl, A., Schlierf, A., et al. (2020) · Science Signaling · doi:10.1126/scisignal.aav1256 · Cited by 27
When Ubiquitin Meets NF-κB: A Trove for Anti-cancer Drug Development
Wu, Z., & Shi, Y. (2013) · Current Pharmaceutical Design · doi:10.2174/1381612811319180010 · Cited by 26
Roles of the two distinct proteasome pathways in hepatitis C virus infection
Shoji, I. (2012) · World Journal of Virology · doi:10.5501/wjv.v1.i2.44 · Cited by 25
Linear ubiquitin assembly complex regulates lung epithelial–driven responses during influenza infection
Brazee, P. L., Morales‐Nebreda, L., Magnani, N., Garcia, J. G. N., Misharin, A. V., Ridge, K. M., Budinger, G. R. S., Iwaï, K., Dada, L. A., & Sznajder, J. I. (2019) · Journal of Clinical Investigation · doi:10.1172/jci128368 · Cited by 22
RNF31 Regulates Skin Homeostasis by Protecting Epidermal Keratinocytes from Cell Death
Tang, Y., Tu, H., Liu, G., Zheng, G., Wang, M., Li, L., Zhao, X., & Lin, X. (2018) · The Journal of Immunology · doi:10.4049/jimmunol.1800172 · Cited by 23
Single-Domain Antibodies as Crystallization Chaperones to Enable Structure-Based Inhibitor Development for RBR E3 Ubiquitin Ligases
Tsai, Y. I., Johansson, H., Dixon, D. P., Martin, S. R., Chung, C., Clarkson, J., House, D., & Rittinger, K. (2019) · Cell chemical biology · doi:10.1016/j.chembiol.2019.11.007 · Cited by 24
Molecular biology of autoinflammatory diseases
Masumoto, J., Zhou, W., Morikawa, S., Hosokawa, S., Taguchi, H., Yamamoto, T., Kurata, M., & Kaneko, N. (2021) · Inflammation and Regeneration · doi:10.1186/s41232-021-00181-8 · Cited by 26
RIP kinases and necroptosis in aging and aging-related diseases
Yang, Y., Li, X., Zhang, T., & Xu, D. (2022) · Life Medicine · doi:10.1093/lifemedi/lnac003 · Cited by 27
Linear Ubiquitination Mediates EGFR-Induced NF-κB Pathway and Tumor Development
Hua, F., Hao, W., Wang, L., & Li, S. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222111875 · Cited by 26
Non-conventional functions for NF-κB members: the dark side of NF-κB
Espinosa, L., Margalef, P., & Bigas, A. (2014) · Oncogene · doi:10.1038/onc.2014.188 · Cited by 25
The fructose-2,6-bisphosphatase TIGAR suppresses NF-κB signaling by directly inhibiting the linear ubiquitin assembly complex LUBAC
Tang, Y., Kwon, H., Neel, B. A., Meron, M. K., Pessin, J. B., Yamada, E., & Pessin, J. E. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.002727 · Cited by 23
Down-Regulation of LOC645166 in T Cells of Ankylosing Spondylitis Patients Promotes the NF-κB Signaling via Decreasingly Blocking Recruitment of the IKK Complex to K63-Linked Polyubiquitin Chains
Yu, H.-C., Huang, K., Lu, M., Tseng, H.-Y. H., Liu, S.-Q., Lai, N., & Huang, H. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.591706 · Cited by 23
Quantitative Phospho-proteomic Analysis of TNFα/NFκB Signaling Reveals a Role for RIPK1 Phosphorylation in Suppressing Necrotic Cell Death
Mohideen, F., Paulo, J. A., Ordureau, A., Gygi, S. P., & Harper, J. W. (2017) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m117.068189 · Cited by 23
Ubiquitination Is Essential for Avibirnavirus Replication by Supporting VP1 Polymerase Activity
Wu, H., Shi, L., Zhang, Y., Peng, X., Zheng, T., Li, Y., Hu, B., Zheng, X., & Zhou, J. (2018) · Journal of Virology · doi:10.1128/jvi.01899-18 · Cited by 24
NLRP10 Affects the Stability of Abin-1 To Control Inflammatory Responses
Mirza, N., Sowa, A. S., Lautz, K., & Kufer, T. A. (2018) · The Journal of Immunology · doi:10.4049/jimmunol.1800334 · Cited by 22
LUBAC-mediated linear ubiquitination in tissue homeostasis and disease
Sasaki, K., & Iwaï, K. (2023) · The Journal of Biochemistry · doi:10.1093/jb/mvad045 · Cited by 24
A de novo dominant-negative variant is associated with OTULIN-related autoinflammatory syndrome
Takeda, Y., Ueki, M., Matsuhiro, J., Walinda, E., Tanaka, T., Yamada, M., Fujita, H., Takezaki, S., Kobayashi, I., Tamaki, S., et al. (2024) · The Journal of Experimental Medicine · doi:10.1084/jem.20231941 · Cited by 22
SIPL1-facilitated PTEN ubiquitination contributes to its association with PTEN
Melo, J. D., Lin, X., He, L., Wei, F., Major, P. P., & Tang, D. (2014) · Cellular Signalling · doi:10.1016/j.cellsig.2014.08.013 · Cited by 23
Mutually exclusive roles of SHARPIN in integrin inactivation and NF-κB signaling
De Franceschi, N., Peuhu, E., Parsons, M., Rissanen, S., Vattulainen, I., Salmi, M., Ivaska, J., & Pouwels, J. (2015) · PLOS ONE · doi:10.1371/journal.pone.0143423 · Cited by 22
Roles of c-IAP Proteins in TNF Receptor Family Activation of NF-κB Signaling
Varfolomeev, E. E., Goncharov, T., & Vucic, D. (2015) · Methods in molecular biology · doi:10.1007/978-1-4939-2422-6_15 · Cited by 21
HOIL‐1‐catalysed, ester‐linked ubiquitylation restricts IL‐18 signaling in cytotoxic T cells but promotes TLR signalling in macrophages
Petrova, T., Zhang, J., Nanda, S. K., Figueras‐Vadillo, C., & Cohen, P. (2021) · FEBS Journal · doi:10.1111/febs.15896 · Cited by 19
Molecular and structural insight into lysine selection on substrate and ubiquitin lysine 48 by the ubiquitin-conjugating enzyme Cdc34
Suryadinata, R., Holien, J. K., Yang, G., Parker, M. W., Papaleo, E., & Šarčević, B. (2013) · Cell Cycle · doi:10.4161/cc.24818 · Cited by 23
Tankyrase-mediated ADP-ribosylation is a regulator of TNF-induced death
Liu, L., Sandow, J. J., Pedrioli, D. M. L., Samson, A. L., Silke, N., Kratina, T., Ambrose, R. L., Doerflinger, M., Hu, Z., Morrish, E., et al. (2022) · Science Advances · doi:10.1126/sciadv.abh2332 · Cited by 24
Activation of the I B kinase complex by HTLV-1 Tax requires cytosolic factors involved in Tax-induced polyubiquitination
Shibata, Y., Tanaka, Y., Gohda, J., & Inoue, J.-I. (2011) · The Journal of Biochemistry · doi:10.1093/jb/mvr106 · Cited by 25
Determinants of E2-ubiquitin conjugate recognition by RBR E3 ligases
Martino, L., Brown, N. R., Masino, L., Esposito, D., & Rittinger, K. (2018) · Scientific Reports · doi:10.1038/s41598-017-18513-5 · Cited by 21
Structural insights into non-covalent ubiquitin activation of the cIAP1-UbcH5B∼ubiquitin complex
Patel, A., Sibbet, G. J., & Huang, D. T. C. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.006045 · Cited by 21
A missense variant in SHARPIN mediates Alzheimer’s disease-specific brain damages
Park, J. Y., Lee, D., Lee, J. J., Gim, J., Gunasekaran, T. I., Choi, K. Y., Kang, S., Do, A. R., Jo, J., Park, J., et al. (2021) · Translational Psychiatry · doi:10.1038/s41398-021-01680-5 · Cited by 21
Trial Watch: Proteasomal inhibitors for anticancer therapy
Obrist, F., Manic, G., Kroemer, G., Vitale, I., & Galluzzi, L. (2014) · Molecular & Cellular Oncology · doi:10.4161/23723556.2014.974463 · Cited by 22
Role of Linear Ubiquitination in Health and Disease
Brazee, P. L., Dada, L. A., & Sznajder, J. I. (2016) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/rcmb.2016-0014tr · Cited by 22
Characterization of RING-Between-RING E3 Ubiquitin Transfer Mechanisms
Reiter, K. H., & Klevit, R. E. (2018) · Methods in molecular biology · doi:10.1007/978-1-4939-8706-1_1 · Cited by 21
Sharpin suppresses β1-integrin activation by complexing with the β1 tail and kindlin-1
Gao, J., Bao, Y., Ge, S., Sun, P., Sun, J., Liu, J., Chen, F., Han, L., Cao, Z., Qin, J., et al. (2019) · Cell Communication and Signaling · doi:10.1186/s12964-019-0407-6 · Cited by 20
Molecular basis for specificity of the Met1-linked polyubiquitin signal
Elliott, P. R. (2016) · Biochemical Society Transactions · doi:10.1042/bst20160227 · Cited by 23
Integrin Regulators in Neutrophils
Pulikkot, S., Hu, L., Chen, Y., Sun, H., & Fan, Z. (2022) · Cells · doi:10.3390/cells11132025 · Cited by 21
Systems Approaches to Dissecting Immunity
Diercks, A. H., & Aderem, A. A. (2012) · Current topics in microbiology and immunology · doi:10.1007/82_2012_246 · Cited by 18
Linear ubiquitination in NF-κB signaling and inflammation: What we do understand and what we do not
Verhelst, K., Verstrepen, L., Carpentier, I., & Beyaert, R. (2011) · Biochemical Pharmacology · doi:10.1016/j.bcp.2011.07.066 · Cited by 19
Essential role of the linear ubiquitin chain assembly complex and TAK1 kinase in A20 mutant Hodgkin lymphoma
Song, Z., Wei, W., Xiao, W., Al-Saleem, E. D., Nejati, R., Chen, L., Yin, J., Fabrizio, J., Petrus, M. N., Waldmann, T. A., et al. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2014470117 · Cited by 19
A functional variant of SHARPIN confers increased risk of late-onset Alzheimer’s disease
Asanomi, Y., Shigemizu, D., Akiyama, S., Miyashita, A., Mitsumori, R., Hara, N., Ikeuchi, T., Niida, S., & Ozaki, K. (2022) · Journal of Human Genetics · doi:10.1038/s10038-021-00987-x · Cited by 19
Linear Polyubiquitin Chain Modification of TDP-43-Positive Neuronal Cytoplasmic Inclusions in Amyotrophic Lateral Sclerosis
Nakayama, Y., Tsuji, K., Ayaki, T., Mori, M., Tokunaga, F., & Ito, H. (2020) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/nlz135 · Cited by 18
Self-citation
LUBAC enables tumor-promoting LTβ receptor signaling by activating canonical NF-κB
Chen, Y., Rieser, E., Bhamra, A., Šurinová, S., Kreuzaler, P. A., Ho, M.-H., Tsai, W., Peltzer, N., de Miguel, D., & Walczak, H. (2024) · Cell Death and Differentiation · doi:10.1038/s41418-024-01355-w · Cited by 18
Viruses utilize ubiquitination systems to escape TLR/RLR-mediated innate immunity
Huang, S., Cheng, A., Wang, M., Yin, Z., Huang, J., & Jia, R. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.1065211 · Cited by 20
Involvement of heterologous ubiquitination including linear ubiquitination in Alzheimer’s disease and amyotrophic lateral sclerosis
Sato, Y., Terawaki, S., Oikawa, D., Shimizu, K., Okina, Y., Ito, H., & Tokunaga, F. (2023) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2023.1089213 · Cited by 17
Self-citation
LUBAC-mediated M1 Ub regulates necroptosis by segregating the cellular distribution of active MLKL
Weinelt, N., Wächtershäuser, K. N., Celik, G., Jeiler, B., Gollin, I., Zein, L., Smith, S. M., Andrieux, G., Das, T., Roedig, J., et al. (2024) · Cell Death and Disease · doi:10.1038/s41419-024-06447-6 · Cited by 19
Keeping Cell Death in Check: Ubiquitylation-Dependent Control of TNFR1 and TLR Signaling
Griewahn, L., Köser, A., & Maurer, U. (2019) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2019.00117 · Cited by 18
Protein Kinase-Mediated Decision Between the Life and Death
Engin, A. (2021) · Advances in experimental medicine and biology · doi:10.1007/978-3-030-49844-3_1 · Cited by 20
Mechanistic insights into the subversion of the linear ubiquitin chain assembly complex by the E3 ligase IpaH1.4 of Shigella flexneri
Liu, J., Wang, Y., Wang, D., Wang, Y., Xu, X., Zhang, Y., Li, Y., Zhang, M., Gong, X., Tang, Y., et al. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2116776119 · Cited by 18

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

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

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

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Citations

Cites

Cited by

Related

Metadata

Record

About these checks