IndraLab

Statements


USP14 deubiquitinates DVL. 11 / 11
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"Deubiquitination of Dishevelled by Usp14 is required for Wnt signaling."

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"These data suggest that deubiquitination of Dvl by Usp14 is necessary for the interaction between Fzd and Dvl."

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"Inhibition of USP14 increases Dvl polyubiquitination and significantly impairs downstream Wnt signaling."

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"A recent report has shown that deubiquitination of disheveled (Dvl) by USP14 is required for Wnt signaling."

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"Therefore, deubiquitination of Dvl by Usp14 may occur via their transient interaction during Wnt signal transduction."

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"To test direct deubiquitination of Dvl by Usp14, we performed a ubiquitin chain trimming assay using immunopurified Dvl-ubiquitin conjugates and recombinant Usp14 in a proteasome-free condition (XREF_FIG and XREF_SUPPLEMENTARY)."

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"As a lack of Dvl deubiquitination by Usp14 appears to attenuate Wnt signaling, we proposed that an elevated forward rate of ubiquitination, which will be counteracted by Usp14 activity, might be induced by Wnt3a CM treatment."

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"Effects of USP14 inhibitor IU1 confirmed that inhibition of USP14 by IU1 increases the K4 linked polyubiquitination of Dvl [XREF_BIBR]."

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"As inhibition of Usp14 activity increased Dvl polyubiquitination, we examined whether knockdown of Usp14 has any effect on Wnt signaling."

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"Contrary to its established mechanistic role, Usp14 mediates deubiquitination of Dvl without a requirement for its UBL domain."

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"The inhibition of USP14 can also increase the degree of ubiquitination of Dvl and significantly inhibit the downstream of Wnt signal transduction [XREF_BIBR]."