IndraLab

"OTUD7B directly interacts with IRF3 and activates p62 by removing K63 polyubiquitin chains leading to enhanced p62 oligomerization."

"Mechanistically, OTUD7B interacts with IRF3, and activates IRF3-associated cargo receptor SQSTM1/p62 (sequestosome 1) by removing its K63-linked poly-ubiquitin chains at lysine 7 (K7) to enhance SQSTM1 oligomerization."

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"RNF26 played a role in EGFR‐driven cell proliferation by ubiquitinating Sqstm1, [ xref ] while mutation of Sqstm1 at K420 led to abnormal ubiquitination and thus inhibited autophagy. [ xref ] TRIM21 could bind to the PB1 domain to ubiquitinate K7, hindering the oligomerization of Sqstm1 and inhibiting its function. [ xref ] CUL5‐ASB6 complex promoted the ubiquitination of Sqstm1 for degradation to inhibit cell proliferation and autophagy. [ xref ] In addition, RNF166 and NEDD4 activated autophagy through ubiquitination of Sqstm1. [ xref ] KEAP1‐CUL3 ubiquitinated Sqstm1 at the site of K420 within the UBA domain, improved the efficiency of substrate transport to the autophagosome, enhanced selective autophagic flux, and accelerated the degradation of target proteins. [ xref ] The ubiquitin‐specific peptidase USP8 acted as a negative regulator of autophagy by deubiquitinating Sqstm1 at K420. [ xref ] The deubiquitinating enzyme OTUD7B interacted with IRF3 to remove the polyubiquitin chain at the K7 site of Sqstm1 to enhance the oligomerization for the block of antiviral immune response. [ xref ] In this study, we found that RNF6, an E3 ubiquitin ligase, mediated the ubiquitination of Sqstm1 at K314 to promote autophagy."