IndraLab

Statements

OTUB2 deubiquitinates CD274. 6 / 6
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"Mechanistically, OTUB2 directly interacts with PD-L1 to disrupt the ubiquitination and degradation of PD-L1 in the endoplasmic reticulum."
38167274
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"To determine whether OTUB2-mediated PD-L1 stabilization is regulated by deubiquitination, we asked whether OTUB2 deubiquitinates PD-L1 to increase protein stability."
38167274
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"We analyzed PD-L1 ubiquitination in the presence of the proteasome inhibitor MG132 and found that MG132-induced PD-L1 ubiquitination was abolished by OTUB2 OE (Fig. 4a)."
38167274
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"We found that OTUB2 reduced the endogenous K48-linked polyubiquitination of PD-L1 but had no effect on K63-linked polyubiquitination (Fig. 4f, g)."
38167274
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"We constructed two mutants, PD-L1ΔICD (devoid of the ICD) and PD-L1 3KR (three lysine residues were mutated to arginine), and examined whether OTUB2 could still reduce the polyubiquitination of PD-L1."
38167274
reach
"OTUB2 can interact with PD-L1 and deubiquitinate and stabilize the PD-L1 protein by intervening in the ERAD pathway."
38167274