IndraLab

Statements

USP12 binds WDR48 and WDR20. 22 / 22
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"Firstly, we confirm the presence of the Usp12, Uaf-1, and WDR20 complex in PC cells and demonstrate the importance of Uaf-1 and WDR20 for Usp12 stabilisation."
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"While the Pinky Finger of USP12 in the UAF1, USP12, and WDR20 complex adopts the same beta-strand conformation as seen in the UAF1 and USP12 complex, F219 on the PK Helix becomes embedded in its pocket formed between the Fingers and Palm domains, instead of being tucked underneath the Fingers domain (XREF_FIG, XREF_FIG, XREF_FIG)."
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"Our structures reveal that UAF1 and WDR20 interact with USP12 at two distinct sites far away from its catalytic center."
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"For example, silencing of USP12 cofactors, Usp1-associated factor 1 (UAF1), or WD repeat domain 20 (WDR20), could influence the UAF1/WDR20/USP12 complex, thus inhibiting USP12 activity and AR-mediated transcription, leading to attenuated colony formation and promoting apoptosis [105]."
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"The USP46-WDR48-WDR20 and the USP12-WDR48-WDR20 complex have a very comparable overall structure."
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"Overall, the UAF1, USP12, and WDR20 complex is distinguished from the two free USP12 structures and the two UAF1 and USP12 complex structures by the apparent stabilization of most flexible structural elements found in the DUB enzyme."
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"Overall these results highlight the potential importance of the Usp12, Uaf-1, and WDR20 complex in AR regulation and PC progression."
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"Highlights : Androgen receptor is a key transcriptional regulator in prostate cancer Usp12, Uaf-1, and WDR20 complex plays a crucial role in androgen receptor stability and activity Destabilising an individual Usp12, Uaf-1, and WDR20 complex member reduces the protein levels of the whole complex and diminishes androgen receptor activity Protein levels of all members of the Usp12, Uaf-1, and WDR20 complex are significantly increased in PC INTRODUCTION."
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"During revision of this manuscript, a structure for the USP12, UAF1, and WDR20 complex was published."
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"Olazabal-Herrero et al (88) revealed that WDR20 facilitates shuttling of the USP12/UAF1/WDR20 complex between the plasma membrane, cytoplasm and nucleus via the CRM1 pathway, which requires the N-terminal motif of USP12 and the novel NES of WDR20.7."
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"Thus, the steady-state localization of the USP46/UAF1/WDR20 complex was cytoplasmic, while the USP12/UAF1/WDR20 complex localized mainly to the plasma membrane (PM)."
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"Furthermore, our data suggest that a previously reported NES in USP12 ( Sanyal, 2016 ) does not act as a relevant nuclear export determinant, and we identify a novel functional NES in WDR20 that media[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"Co-expressed YFP-USP12/UAF1-mRFP/Myc-WDR20 co-localized to the PM ( Fig. 2 d), whereas YFP-USP46/UAF1-mRFP/Myc-WDR20 diffusely co-localized in the cytoplasm.Altogether, these results suggest that WDR2[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"Binding of WDR20 to the UAF1-USP12 complex induces multiple structural changes in the enzyme, converting it into a compact form similar to Ub-bound USP46."
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"The overall structure of the USP46-WDR48-WDR20 complex is very similar to that of the USP12-WDR48-WDR20 complex."
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"WDR20 does not present any alpha helical region according to the reported structure of the USP12/UAF1/WDR20 complex ( Li et al., 2016 )."
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"Moreover, WDR20 plays a crucial role in modulating the USP12-UAF1-WDR20 complex shuttling between the plasma membrane, cytoplasm, and nucleus [46]."
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"Unfortunately, the currently available structure of the USP12/UAF1/WDR20 complex does not provide information on the extreme amino-terminal end of USP12."
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"We hypothesise that targeting the Usp12, Uaf-1, and WDR20 complex in a similar manner would allow development of therapeutics with greater specificity and sensitivity than targeting Usp12 alone."
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"Recent structural insights into the USP46 and UAF1 complex and the USP12, UAF1, and WDR20 complex revealed that the activators interact with surfaces remote from the catalytic center and mediate activation via long-range allosteric mechanisms."
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"Although the WDR20 region containing the NES is not solved in the currently available structure of the USP12/UAF1/WDR20 complex, these results suggest that the WDR20 NES is accessible for CRM1 interac[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"Mechanisms that may modulate WDR20 localization, such as post-translational modification, might in turn modulate the localization of DUB complexes containing this subunit.Our results support a model ([MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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