TSG101 Physically Interacts with Linear Ubiquitin Chain Assembly Complex (LUBAC) and Upregulates the TNFα-Induced NF-κB Activation

• Published in: Molecules and cells pp. 430 - 440
• Main Authors: 최의주, Eunju Kim, Hyunchu Cho, Gaeul Lee, Heawon Baek, In Young Lee
• Format: Journal Article
• Language: English
• Published: 한국분자세포생물학회 01.07.2023
• Subjects: 생물학
• ISSN: 1016-8478; 0219-1032
• DOI: 10.14348/molcells.2023.0029

Linear ubiquitin chain assembly complex (LUBAC) is a ubiquitin E3 ligase complex composed of HOIP, HOIL-1L, and SHARPIN that catalyzes the formation of linear/M1- linked ubiquitin chain. It has been shown to play a pivotal role in the nuclear factor (NF)-κB signaling induced by proinflammatory stimuli. Here, we found that tumor susceptibility gene (TSG101) physically interacts with HOIP, a catalytic component of LUBAC, and potentiates LUBAC activity. Depletion of TSG101 expression by RNA interference decreased TNFα-induced linear ubiquitination and the formation of TNFα receptor 1 signaling complex (TNFRSC). Furthermore, TSG101 facilitated the TNFα-induced stimulation of the NF-κB pathway. Thus, we suggest that TSG101 functions as a positive modulator of HOIP that mediates TNFα-induced NF-κB signaling pathway. KCI Citation Count: 0