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USP26 deubiquitinates SMAD7. 4 / 5
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"USP26 deubiquitinates SMAD7."

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"The deubiquitinating enzyme USP26 deubiquitinates and stabilizes SMAD7 allowing SMAD7 to act as scaffold to recruit the HECT-E3 ligase SMURF2 to the TGFβ receptor complex, facilitating ubiquitin-mediated proteasomal degradation of the receptor complex and attenuating TGFβ signalling ."

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"Interestingly, glioblastoma patients with low expression levels of USP26 have a worse prognosis, which correlates with in vitro experiments where knock-down of USP26 leads to increased phospho-SMAD2, and cell migration [63]; since USP26 de-ubiquitinates and stabilizes SMAD7, this leads to downregulation of TGF-β activity."

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"Examples include ubiquitin specific protease 10 (USP10), which can act on SMAD4 to make it deubiquitinated and stable, further promoting TGF-beta signaling [XREF_BIBR], and USP26, which promotes SMAD7 deubiquitination, thereby amplifying the inhibitory effect of SMAD7 and strengthening the inhibition of the TGF-beta signaling pathway [XREF_BIBR]."