IndraLab

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USP7 deubiquitinates TRIM27. 5 / 5
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"Although the deubiquitylation of TRIM27 by binding USP7 for WASH-mediated precise actin polymerization has previously been identified, how their complex formation is regulated remains obscure."
37307465
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"Our findings suggest that <span class="match term0">USP7</span> acts as a negative regulator in antiviral signaling by stabilizing <span class="match term1">TRIM27</span> and promoting the degradation of TBK1"
29688809
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"First, USP7 deubiquitinates TRIM27 to prevent its own auto-degradation and thus stabilizes the complex."
28626083
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"On the other hand, the interaction between USP7 and TRIM27 (another E3 ubiquitin ligase) results in multiple outcomes: USP7 not only deubiquitylates TRIM27, but the latter in turn, binds to and ubiquitylates USP7, which facilitates recruitment and deubiquitylation of another protein, RIP1 by USP7 [33]."
36342772
reach
"On the other hand, USP7 prevents TRIM27 auto-ubiquitination and subsequent degradation (Hao et al. 2013)."
36538041