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WDR48 activates USP46. 24 / 24
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"WDR48 stimulates the activity of three DUBs, USP12, USP46 and USP1, a DUB which regulates the Fanconi anemia DNA damage pathway."

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"Although mammalian USP46 and USP12 DUB activity can be stimulated by two proteins UAF-1 and WDR20, the C. elegans homologs of these genes have not yet been identified."

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"The WD-repeat protein WDR48 (USP1 associated factor UAF-1) stimulates activity of ubiquitin specific proteases USP1, USP12, and USP46."

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"WDR48 stimulates the activity of three DUBs, USP12, USP46 and USP1, a DUB which regulates the Fanconi anemia DNA damage pathway (Cohn et al., 2007 (Cohn et al., , 2009 Faesen et al., 2011) ."

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"Therefore, this suggests that for some USPs the KG FP reagent may be a better substrate, and provide more relevant kinetic parameters.This study confirmed that the modulator UAF1 activates USP1, USP12[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

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"For example, USP1, USP12, and USP46 are activated by the WD40-repeat containing UAF1, and USP7 is activated by GMPS (Cohn et al., 2007, 2009; Faesen et al., 2011; van der Knaap et al., 2005)."

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"Together, UAF1 and WDR20 are able to synergistically stimulate the enzymatic activities of USP12 and USP46 to a peak level."

sparser
"However, a structural comparison of the enzyme in these two post-reaction forms revealed few conformational differences, leaving the mechanism of USP46 activation by UAF1 elusive."

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"WDR48 and UAF1 is an activator of USP1 and more recently has been shown to activate USP12 and USP46."

sparser
"UAF1 also binds and activates two other DUBs, USP12 and USP46 ( xref ), and studies that reveal how UAF1 binds and activates USP12 and USP46 suggest that UAF1 will bind to USP1 in an analogous manner ( xref , xref )."

sparser
"However, as shown previously for USP46/UAF1 ( xref ), the combination of these complementary mutants rescues the activation ( xref f), highlighting the importance of the fingers sub domain in USP12 and USP46 ( xref ) activation by UAF1."

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"Both WDR48 and WDR20 stimulate USP12 and USP46 catalytic activity (k cat) without increasing substrate binding affinity, suggesting that the WDR proteins may affect DUB activity via a novel structural mechanism."

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"Structural insights into the activation of USP46 by WDR48 and WDR20."

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"We found that USP-46 is ubiquitinated and that expression of WDR-48 reduces the levels of ubiquitin-USP-46 conjugates and increases the half-life of USP-46."

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"Interestingly, the Caenorhabditis elegans homologs of WDR20 and WDR48 (also known as UAF1) can bind to and activate USP46."

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"Interestingly, USP12 and USP46 are activated by two β-propeller proteins, UAF1, and WDR20."

sparser
"This study confirmed that the modulator UAF1 activates USP1, USP12, and USP46, and GMPS activates USP7."

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"We found that increased expression of WDR-48, but not WDR-20, promotes USP-46 abundance in mammalian cells in culture and in C. elegans neurons in vivo Inhibition of the proteasome increased USP-46 abundance, and this effect was non additive with increased WDR-48 expression."

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"However, a structural comparison of the enzyme in these two post-reaction forms revealed few conformational differences, leaving the mechanism of USP46 activation by UAF1 elusive."

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"WDR48 stimulates the activity of three DUBs, USP12, USP46 and USP1, a DUB which regulates the Fanconi anemia DNA damage pathway (Cohn et al., 2007, 2009; Faesen et al., 2011)."

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"UAF1 stimulates not only USP1, but also two other DUB enzymes, USP12 and USP46."

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"Since UAF1 stimulates the deubiquitinating activity of USP1 and USP46 [XREF_BIBR, XREF_BIBR], we speculate that UAF1 and ubiquitin can simultaneously bind to opposite surfaces of the Fingers sub-domain in these DUBs."

sparser
"Interestingly, USP12 and USP46 are activated by two β-propeller proteins, UAF1, and WDR20."

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"Given the distinct binding mode elucidated here, it is less straightforward to reconcile this structure with direct active-site modulation, yet we propose a mechanism centered on WDR48 dependent USP s[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"