IndraLab

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USP36 deubiquitinates DOCK4. 5 / 5
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"USP36 deubiquitinates the dedicator of cytokinesis 4 (DOCK4), as evidenced by the up- or downregulation of Usp36 in TECs in response to overexpression or knockdown, respectively [144]."
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"Further investigation into the mechanisms proved that USP36 could directly bind to and mediate the deubiquitination of dedicator of cytokinesis 4 (DOCK4), a guanine nucleotide exchange factor (GEF) that could activate Wnt/beta-catenin signaling pathway and induce EMT."
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"Further, we found that USP36 could directly bind to and mediate the deubiquitination of dedicator of cytokinesis 4 (DOCK4), a guanine nucleotide exchange factor (GEF) that could activate Wnt/β-catenin signaling pathway and induce EMT."
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"USP36 contributes to DN progression by directly deubiquitinating cytokinin 4 (DOCK4) and aggravating guanine nucleotide exchange factor (GEF)-mediated EMT (136) ( Table 9 ).2.8.5 Roles of USPs in diabetic neuropathic pain."
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"Additionally, USP36 directly bound to and mediated the de-ubiquitination of DOCK4, whereas DOCK4 knockdown effectively abolished EMT induced by USP36 overexpression through suppressing Wnt/β-catenin signaling in TECs (Zhu et al., 2021)."
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