RNF126 is a positive regulator of TRAF3 ubiquitination

Ubiquitination and deubiquitination of signaling molecules are critical regulatory mechanisms in various biological contexts such as inflammatory signaling and the DNA damage response. Thus, finely tuned regulation of protein ubiquitination is essential for maintaining cellular homeostasis. Here, we...

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Published inBioscience, biotechnology, and biochemistry Vol. 85; no. 12; pp. 2420 - 2428
Main Authors Kim, Soomi, Park, Kibeom, Oh, Jung-Min, Kim, Hongtae
Format Journal Article
LanguageEnglish
Published England 01.12.2021
Subjects
TNF Receptor-Associated Factor 3
RNF126
TRAF3
ubiquitination
antiviral response
OTUB1
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Summary:Ubiquitination and deubiquitination of signaling molecules are critical regulatory mechanisms in various biological contexts such as inflammatory signaling and the DNA damage response. Thus, finely tuned regulation of protein ubiquitination is essential for maintaining cellular homeostasis. Here, we showed that the RING finger protein RNF126 interacts with TRAF3 and promotes its K63-linked polyubiquitination, which is a crucial step in the TRAF3-dependent antiviral response. We found that RNF126 also interacts with OTUB1, a deubiquitinating enzyme that negatively regulates K63-linked ubiquitination of TRAF3. RNF126 promotes ubiquitination of OTUB1, leading to reduced deubiquitinating activity toward TRAF3. Moreover, RNF126 promotes ubiquitination of OTUB1 on cysteine 91, which is reportedly required for its catalytic activity. Taken together, our results suggest that RNF126 positively regulates the antiviral response by directly promoting K63-linked polyubiquitination of TRAF3 and by reducing OTUB1 activity.
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ISSN:1347-6947
1347-6947
DOI:10.1093/bbb/zbab177