IndraLab

Statements


USP28 deubiquitinates MYC. 8 / 8
1 1 | 6

"Usp28, an ubiquitin-specific protease, binds to myc through an interaction with fbw7alpha, an f-box protein that is part of an scf-type ubiquitin ligase. Therefore, it stabilizes myc."

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"Recent evidence has revealed that c-Myc can be deubiquitylated and regulated by USP28, USP36 and USP37."

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"The resultant weakly acidic microenvironment enhances the deubiquitination of MYC by USP28, improves the stability of MYC, and activates the promoter of Slug, ultimately promoting the stem cell-like properties of breast cancer."

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"The product of this is lactic acid that changes the pH of the local environment which then promotes the formation of a weakly acidic microenvironment, thus consequently enhancing the deubiquitination of MYC by the deubiquitination enzyme USP28 and improving the stability of MYC [38]."

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"USP28 directly deubiquitinates and stabilizes MYC."

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"An early study showed that USP28 deubiquitinates c-Myc via interacting with Fbw7alpha whereas a recent study reveals that USP37 deubiquitinates c-Myc independently of Fbw7 and c-Myc phosphorylation."

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"Identified in a retroviral shRNA library screen, USP28 has been shown to decrease MYC polyubiquitination and increase MYC stability by antagonizing the activity of the SCF FBW7 ubiquitin ligase complex [XREF_BIBR]."