IndraLab

Statements

USP12 binds WDR20. 22 / 39
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"Binding of WDR20 to the UAF1 and USP12 complex induces multiple structural changes in the enzyme, converting it into a compact form similar to Ub bound USP46."
27373336
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"Usp12, Uaf-1 and WDR20 form a complex acting within a positive feedback loop in PC cells."
26462181
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"Altogether, our findings suggest a model whereby mutually exclusive binding of DMWD and WDR20 to USP12 may lead to formation of deubiquitinase complexes with distinct subcellular localization, potentially targeting different substrate repertoires."
33844468
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"It is possible that binding of PHLPP or PHLPPL to Uaf-1 requires a conformational change that is facilitated by Uaf-1 becoming part of the WDR20 and Usp12 complex."
25216524
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"The partial overlap of the binding interfaces and the high affinity of WDR20 suggests that WDR20 binding to USP12 and UAF1 can either prevent binding of the second UAF1 molecule or it can actively compete out UAF1 if it is bound to the USP12 and UAF1 complex."
27650958
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"Results confirmed the interaction between endogenous Usp12, Uaf-1 and WDR20 in PC cells."
26462181
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"As both Uaf-1 and WDR20 interact with Usp12 we hypothesised that Uaf-1 and WDR20 would also be found in a complex with AR."
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"Together, these results indicate that the amino-terminal 1 MEIL 4 motif is necessary for the efficient recruitment of USP12/WDR20 to the PM, but is not sufficient to confer PM localization to a USP46/[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
30466959
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"To address this possibility, we made use of the information provided by a recent study ( Li et al., 2016 ), where the three-dimensional structure of a ternary USP12/UAF1/WDR20 complex was reported, id[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"The calculated halftime of recovery (t 1/2 ) and mobile fraction (F m ) values were 19.44 s and 65.29%, respectively, indicating that the PM localization of YFP-USP12 is highly dynamic.Together with t[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"These observations indicate that the USP12/WDR20 complex is able to dynamically shuttle between PM, cytoplasm and nucleus.The USP12 motif 77 KESLLTCLADLFHSI 91 ( Fig. 6 a) has been recently proposed t[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"Besides, USP12 and USP46 can also bind with WDR20 but USP1 cannot; and the activity of USP12 and USP46 can be activated by WDR48 and WDR20 independently and synergistically [38, 39]."
37752518
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"This observation suggests that, in the absence of a strong NLS in USP12, recruitment to the PM largely prevails over slow diffusion into the nucleus upon formation of a USP12/WDR20 complex.On the othe[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"We confirmed that “NES” mutations disrupt USP12/WDR20 interaction."
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"WDR20 interacts with the USP12 Palm domain, and it is paralleled with the WD40 repeat domain of UAF1 ( xref E)."
33498168
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"Our structures reveal that UAF1 and WDR20 interact with USP12 at two distinct sites far away from its catalytic center."
27373336
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"WDR20 binding to USP12 and USP46 showed a significant increase in the catalytic activity in vitro [71,76]."
32512887
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"It might be argued that co-expression of WDR20 might indirectly promote PM recruitment without requiring the formation of a USP12/WDR20 complex."
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"USP12 binds to Uaf-1 and WDR20 to form a complex to deubiquitinate AR, thereby increasing AR protein stability and transcriptional activity, while the depletion of WDR20 and Uaf-1 displays the opposite effect."
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"In the two UAF1-USP12 complex structures, UAF1 binding appears to induce BL1 destabilization via a chain of conformational changes, whereas the WDR20-USP12 interaction seems to overwrite the allosteric effect of UAF1 by re-stabilizing the loop."
27373336
sparser
"The second UAF1 binding site has low affinity and partially overlaps the WDR20-USP12 binding interface, thus the binding of WDR20 to USP12/UAF1 may prevent the second UAF1 molecule from binding to USP12, so it may have a regulatory effect [ xref ]."
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"We generated YFP-USP12 V279D/F287A and Myc-WDR20 F262A/W306A mutants and confirmed that these mutations largely or completely abrogate WDR20 binding to USP12 in 293 T cells ( Fig. 4 a)."
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