IndraLab

Statements

USP40 deubiquitinates Claudin1. 4 / 4
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"Similarly, our study confirmed that Claudin1 is degraded by the ubiquitin–proteasome system in HCC, and USP40 inhibits Claudin1 polyubiquitination to increase its stability.c-Myc is an oncogenic transcription factor participated in biological functions including cancer cell proliferation, EMT, cancer stemness, metastasis, and metabolic reprogramming [24, 25]."
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"Our study reveals that USP40 enhances HCC malignant development by deubiquitinating and stabilizing Claudin1, suggesting that targeting USP40 may be a novel approach for HCC therapy."
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"USP40 could interact with Claudin1 and deubiquitinates Claudin1 to stabilize its protein level."
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"Ubiquitination assay revealed that USP40 knockdown increased the polyubiquitination of Claudin1, whereas USP40 overexpression reduced the polyubiquitination of Claudin1 (Fig. 5G, H)."
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