IndraLab

Statements

UBA1 binds USP13. 5 / 5
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"Although the experimental results showed that USP13-UBA could bind ubiquitin, USP13 still exhibited only weak deubiquitination enzyme activity, which is incompatible with the findings that USP13 can deubiquitinate various important substrates implicated in disease and tumor development ( xref ; xref )."
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"In 2011, Hu et al. reported the solution structure of USP13-UBA (PDB 2LBC)."
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"Albeit no ubiquitin-bound UBA structure is resolved, sequence alignment revealed that USP13-UBA contains an MGF motif that presumably can bind Ub ( xref ), consistent with results from pull-down and ITC experiments ( xref )."
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"In addition, NMR titration data reflected that M664, F666, M739, and F741 might be the key residues responsible for the binding of USP13-UBA to Ub ( xref )."
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"Overall, the USP13-ZnF domain cannot bind to Ub to activate USP13, whereas USP13-UBA can bind, which may partially explain the reason why USP13 displays only weak basal deubiquitination enzyme activity: the binding sites of USP13 to Ub are less than that other USP members, thus providing weaker binding affinity and consequent cleavage activity towards ubiquitin chains; There possibly exists constitutive self-inhibition for full-length USP13 supported by the interaction of UBA with ZnF domain, which is hypothesized to be released by recruitment of other proteins or modification, such as phosphorylation."
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