bioRxiv preprint doi: https://doi.org/10.1101/830380; this version posted November 4, 2019. The copyright holder for this preprint (which was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under aCC-BY 4.0 International license. Mul1 suppresses Nlrp3 inflammasome activation through ubiquitination and degradation of Asc June-Hyung Kim1, Yunjong Lee1, Gee Young Suh2, Yun-Song Lee1 1. Division of Pharmacology, Department of Molecular & Cellular Biology, Sungkyunkwan University School of Medicine, Suwon, Republic of Korea 2. Department of Critical Care Medicine in Samsung Medical Center, Sungkyunkwan University School of Medicine, Seoul, Republic of Korea Running title: Mul1-mediated Asc ubiquitination Correspondence: Yun-Song Lee, M.D., Ph.D. Division of Pharmacology, Department of Molecular & Cellular Biology, Sungkyunkwan University School of Medicine, 2066 Seobu-ro, Jangan-gu, Suwon 16419, Republic of Korea Tel: +82 31-299-6190 Fax: +82 31-299-6209 E-mail:
[email protected] bioRxiv preprint doi: https://doi.org/10.1101/830380; this version posted November 4, 2019. The copyright holder for this preprint (which was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under aCC-BY 4.0 International license. Abstract Activation of the Nlrp3 inflammasome consisting of three major components, Nlrp3, Asc, and pro-caspase-1, results in the activation of caspase-1 and subsequent proteolytic cleavage of pro-IL-1β and pro-IL-18. To avoid excessive inflammatory response, the Nlrp3 inflammasome has to be precisely controlled.