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Kim, Hongtae
Cancer/DNA damage Lab.
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dc.citation.endPage 2428 -
dc.citation.number 12 -
dc.citation.startPage 2420 -
dc.citation.volume 85 - Kim, Soomi - Park, Kibeom - Oh, Jung-Min - Kim, Hongtae - 2023-12-21T15:06:35Z - 2023-12-21T15:06:35Z - 2021-10-26 - 2021-12 -
dc.description.abstract Ubiquitination and de-ubiquitination 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 poly-ubiquitination, which is a crucial step in the TRAF3-dependent anti-viral 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 towards 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 anti-viral response by directly promoting K63-linked poly-ubiquitination of TRAF3 and by reducing OTUB1 activity. -
dc.identifier.bibliographicCitation BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY, v.85, no.12, pp.2420 - 2428 -
dc.identifier.doi 10.1093/bbb/zbab177 -
dc.identifier.issn 0916-8451 -
dc.identifier.scopusid 2-s2.0-85121033499 -
dc.identifier.uri -
dc.identifier.url -
dc.identifier.wosid 000727719700010 -
dc.language 영어 -
dc.publisher Japan Society for Bioscience Biotechnology and Agrochemistry/Nippon Nogeikagaku Kai -
dc.title RNF126 is a positive regulator of TRAF3 ubiquitination -
dc.type Article -
dc.description.isOpenAccess FALSE -
dc.type.docType Article -
dc.description.journalRegisteredClass scie -
dc.description.journalRegisteredClass scopus -


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