IndraLab

Statements

USP26 inhibits TGFB. 7 / 7
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"As knockdown of USP26 potently activated the TGF-beta pathway in breast cancer, we investigated whether depletion of USP26 in the TGF-beta-responsive metastatic cell line MDA-MB-231 enhanced cellular motility and invasion."
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"USP26 has been found to negatively regulate the TGF-β signaling pathway by deubiquitination and stabilizing SMAD7 in glioblastoma (79)."
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"Taken together, these findings confirmed our hypothesis that loss of USP26 enhances TGF-beta signaling and confers poor prognosis in glioblastoma patients."
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"CYLD and USP26 are found to interact with SMAD7 for its K63-linked polyubiquitination to control TGF-β [69, 70], USP26 deficiency enhances the activation of TGF-β [70]."
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"These results suggest that USP26 may potentially act in conjunction with SMAD7 and SMURF2 to downregulate canonical TGF-beta signaling."
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"Taken together, these data indicate that USP26 inhibits TGF-beta pathway activity by limiting Lys48 ubiquitin mediated degradation of SMAD7 consequently resulting in enhanced ubiquitylation and degradation of the TbetaR complex."
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"In line with our other models, knockdown of USP26 in this patient derived cell line enhanced TGF-beta activity as evidenced by increased levels of phospho-SMAD2 and increased expression of TGF-beta target genes CTGF, LIF, and SMAD7 (Fig XREF_FIG D and E)."
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