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USP3 deubiquitinates MYD88. 4 / 4
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"To further understand how USP3 deubiquitinates the MyD88, we generated an inactive catalytic mutant of USP3 (C168S) and a USP3 mutant (H56A) with a disrupted zinc‐finger structure."
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"Co‐IP data revealed that USP3 co‐expression cannot disrupt the interaction between MyD88 and TRAF6, while the interaction between MyD88 and TAK1 is severely interrupted (Fig EV3L and M), indicating that the deubiquitination of MyD88 by USP3 may interrupt TAK1 recruitment."
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"To test this possibility, we performed ubiquitination assays and found that USP3 markedly reduced both total ubiquitination and the K63‐linked ubiquitination of MyD88."
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"Furthermore, MyD88 underwent K63‐linked ubiquitination after LPS treatment in THP‐1 cells, and USP3 deficiency dramatically enhanced the K63‐linked ubiquitination of MyD88 (Fig 4D)."
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