Biology:LUBAC

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Linear ubiquitin chain assembly complex (LUBAC) is a multi-protein complex and the only known E3 ubiquitin ligase able to conjugate ubiquitin in a head-to-tail manner to generate linear (M1-linked) polyubiquitin chains. The complex is currently known to be composed of three proteins: heme-oxidized IRP2 ubiquitin ligase 1 (HOIL-1), HOIL-1-interacting protein (HOIP), and Shank-associated RH domain-interacting protein (SHARPIN)[1], [2],.[3] HOIL-1 and HOIP are both E3 ubiquitin ligases, however, the specific linear ubiquitin-ligating activity is enacted by HOIP.[4] Mice deficient in HOIP are embryonically lethal.[5] Two cases of mutated HOIP have been detected in humans. These patients presented with autoinflammation and immunodeficiency[6],.[7] HOIL-1 is required for LUBAC assembly and stability as demonstrated by embryonic lethality in HOIL-1 deficient mice.[8] Recently, it has been noted, that HOIL-1 is also able to catalyze formation of oxyester bonds between the C-terminus of ubiquitin and serine/threonine of substrate protein in TLR signaling.[9] SHARPIN exhibits a significant sequence similarity to HOIL-1 and is important for LUBAC stability. Spontaneous point mutation in the Sharpin gene in mice leads to development of chronic proliferative dermatitis (cpdm)[10],.[11] Both HOIL-1 and SHARPIN bind to HOIP through their ubiquitin-like (UBL) domain[1],.[2] LUBAC consisting of either HOIP-HOIL-1 or HOIP-SHARPIN is functional in vitro, however the greatest activity of the complex has been observed in the presence of all three components.[2] LUBAC modulates signaling complexes activating the canonical NF-kB pathway in response to various stimuli (e.g., TNF, IL-1, CD40L) by adding M1-linked polyubiquitin chains to signaling proteins[2],.[12] Additionally, LUBAC has been shown to interact with PKC and NLRP3/ASC inflammasome[13],.[14]

Antagonistic to LUBAC are deubiquitinases such as OTULIN or CYLD, of which OTULIN is the only deubiquitinase that removes M1-linked ubiquitin linkages exclusively.[15]

LUBAC components have been most widely studied in the context of TNF signaling.[citation needed]

References

  1. ↑ 1.0 1.1 Kirisako, Takayoshi; Kamei, Kiyoko; Murata, Shigeo; Kato, Michiko; Fukumoto, Hiromi; Kanie, Masato; Sano, Soichi; Tokunaga, Fuminori et al. (2006-10-18). "A ubiquitin ligase complex assembles linear polyubiquitin chains". The EMBO Journal 25 (20): 4877–4887. doi:10.1038/sj.emboj.7601360. ISSN 0261-4189. PMID 17006537. 
  2. ↑ 2.0 2.1 2.2 2.3 Gerlach, Björn; Cordier, Stefanie M.; Schmukle, Anna C.; Emmerich, Christoph H.; Rieser, Eva; Haas, Tobias L.; Webb, Andrew I.; Rickard, James A. et al. (March 2011). "Linear ubiquitination prevents inflammation and regulates immune signalling" (in en). Nature 471 (7340): 591–596. doi:10.1038/nature09816. ISSN 1476-4687. PMID 21455173. https://www.nature.com/articles/nature09816. 
  3. ↑ Ikeda, Fumiyo; Deribe, Yonathan Lissanu; Skånland, Sigrid S.; Stieglitz, Benjamin; Grabbe, Caroline; Franz-Wachtel, Mirita; van Wijk, Sjoerd J. L.; Goswami, Panchali et al. (March 2011). "SHARPIN forms a linear ubiquitin ligase complex regulating NF-κB activity and apoptosis" (in en). Nature 471 (7340): 637–641. doi:10.1038/nature09814. ISSN 1476-4687. PMID 21455181. 
  4. ↑ Smit, Judith J; Monteferrario, Davide; Noordermeer, Sylvie M; van Dijk, Willem J; van der Reijden, Bert A; Sixma, Titia K (2012-10-03). "The E3 ligase HOIP specifies linear ubiquitin chain assembly through its RING-IBR-RING domain and the unique LDD extension: HOIP RBR-LDD module specifies linear ubiquitin chains" (in en). The EMBO Journal 31 (19): 3833–3844. doi:10.1038/emboj.2012.217. PMID 22863777. 
  5. ↑ Peltzer, Nieves; Rieser, Eva; Taraborrelli, Lucia; Draber, Peter; Darding, Maurice; Pernaute, Barbara; Shimizu, Yutaka; Sarr, Aida et al. (2014-10-09). "HOIP Deficiency Causes Embryonic Lethality by Aberrant TNFR1-Mediated Endothelial Cell Death" (in English). Cell Reports 9 (1): 153–165. doi:10.1016/j.celrep.2014.08.066. ISSN 2211-1247. PMID 25284787. https://www.cell.com/cell-reports/abstract/S2211-1247(14)00742-6. 
  6. ↑ Boisson, Bertrand; Laplantine, Emmanuel; Dobbs, Kerry; Cobat, Aurélie; Tarantino, Nadine; Hazen, Melissa; Lidov, Hart G.W.; Hopkins, Gregory et al. (2015-06-01). "Human HOIP and LUBAC deficiency underlies autoinflammation, immunodeficiency, amylopectinosis, and lymphangiectasia" (in en). Journal of Experimental Medicine 212 (6): 939–951. doi:10.1084/jem.20141130. ISSN 1540-9538. PMID 26008899. PMC 4451137. https://rupress.org/jem/article/212/6/939/41820/Human-HOIP-and-LUBAC-deficiency-underlies. 
  7. ↑ Oda, Hirotsugu; Beck, David B.; Kuehn, Hye Sun; Sampaio Moura, Natalia; Hoffmann, Patrycja; Ibarra, Maria; Stoddard, Jennifer; Tsai, Wanxia Li et al. (2019-03-18). "Second Case of HOIP Deficiency Expands Clinical Features and Defines Inflammatory Transcriptome Regulated by LUBAC". Frontiers in Immunology 10: 479. doi:10.3389/fimmu.2019.00479. ISSN 1664-3224. PMID 30936877. 
  8. ↑ Peltzer, Nieves; Darding, Maurice; Montinaro, Antonella; Draber, Peter; Draberova, Helena; Kupka, Sebastian; Rieser, Eva; Fisher, Amanda et al. (May 2018). "LUBAC is essential for embryogenesis by preventing cell death and enabling haematopoiesis" (in en). Nature 557 (7703): 112–117. doi:10.1038/s41586-018-0064-8. ISSN 1476-4687. PMID 29695863. 
  9. ↑ Kelsall, Ian R.; Zhang, Jiazhen; Knebel, Axel; Arthur, J. Simon C.; Cohen, Philip (2019-07-02). "The E3 ligase HOIL-1 catalyses ester bond formation between ubiquitin and components of the Myddosome in mammalian cells" (in en). Proceedings of the National Academy of Sciences 116 (27): 13293–13298. doi:10.1073/pnas.1905873116. ISSN 0027-8424. PMID 31209050. 
  10. ↑ HogenEsch, H.; Torregrosa, S. E.; Boggess, D.; Sundberg, B. A.; Carroll, J.; Sundberg, J. P. (March 2001). "Increased expression of type 2 cytokines in chronic proliferative dermatitis (cpdm) mutant mice and resolution of inflammation following treatment with IL-12". European Journal of Immunology 31 (3): 734–742. doi:10.1002/1521-4141(200103)31:3<734::aid-immu734>3.0.co;2-9. ISSN 0014-2980. PMID 11241277. https://pubmed.ncbi.nlm.nih.gov/11241277. 
  11. ↑ Seymour, R E; Hasham, M G; Cox, G A; Shultz, L D; HogenEsch, H; Roopenian, D C; Sundberg, J P (July 2007). "Spontaneous mutations in the mouse Sharpin gene result in multiorgan inflammation, immune system dysregulation and dermatitis" (in en). Genes & Immunity 8 (5): 416–421. doi:10.1038/sj.gene.6364403. ISSN 1466-4879. PMID 17538631. https://www.nature.com/articles/6364403. 
  12. ↑ Tokunaga, Fuminori; Sakata, Shin-ichi; Saeki, Yasushi; Satomi, Yoshinori; Kirisako, Takayoshi; Kamei, Kiyoko; Nakagawa, Tomoko; Kato, Michiko et al. (February 2009). "Involvement of linear polyubiquitylation of NEMO in NF-κB activation" (in en). Nature Cell Biology 11 (2): 123–132. doi:10.1038/ncb1821. ISSN 1465-7392. PMID 19136968. http://www.nature.com/articles/ncb1821. 
  13. ↑ Rodgers, Mary A.; Bowman, James W.; Fujita, Hiroaki; Orazio, Nicole; Shi, Mude; Liang, Qiming; Amatya, Rina; Kelly, Thomas J. et al. (2014-06-30). "The linear ubiquitin assembly complex (LUBAC) is essential for NLRP3 inflammasome activation" (in en). Journal of Experimental Medicine 211 (7): 1333–1347. doi:10.1084/jem.20132486. ISSN 1540-9538. PMID 24958845. PMC 4076580. https://rupress.org/jem/article/211/7/1333/41630/The-linear-ubiquitin-assembly-complex-LUBAC-is. 
  14. ↑ Nakamura, Munehiro; Tokunaga, Fuminori; Sakata, Shin-ichi; Iwai, Kazuhiro (December 2006). "Mutual regulation of conventional protein kinase C and a ubiquitin ligase complex" (in en). Biochemical and Biophysical Research Communications 351 (2): 340–347. doi:10.1016/j.bbrc.2006.09.163. PMID 17069764. https://linkinghub.elsevier.com/retrieve/pii/S0006291X06022236. 
  15. ↑ Keusekotten, Kirstin; Elliott, Paul Ronald; Glockner, Laura; Fiil, Berthe Katrine; Damgaard, Rune Busk; Kulathu, Yogesh; Wauer, Tobias; Hospenthal, Manuela Kathrin et al. (June 2013). "OTULIN Antagonizes LUBAC Signaling by Specifically Hydrolyzing Met1-Linked Polyubiquitin" (in en). Cell 153 (6): 1312–1326. doi:10.1016/j.cell.2013.05.014. PMID 23746843. 



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