IndraLab

Statements

UCHL3 binds MTA2. 7 / 7
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"Of note, circ MTA2 could interact with UCHL3, which ultimately reduced the ubiquitination degradation of MTA2 , thus promoting GC progression."
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"Interestingly, CircMTA2 interacts with UCHL3 to promote ubiquitination and stabilization of MTA2 protein by facilitating UCHL3-mediated deubiquitinating, suggesting that CircMTA2 regulates the deubiquinase activity of UCHL3 via acting as protein scaffolds to promote the interaction between UCHL3 and MTA2 [ xref ] (Fig.  xref )."
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"Moreover, overexpression of circMTA2 significantly enhanced the interaction between UCHL3 and MTA2 (Figure 6E) and increased the ubiquitination level of MTA2 (Figure 6F)."
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"Moreover, the Co-IP assays indicated that UCHL3 and MTA2 could bind to each other in AGS and MKN-45 cells ( xref D)."
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"In vitro binding assays indicated that the C1 box domain (90–100 amino acids), but not other domains, of UCHL3 protein specifically bound to MTA2 ( xref G)."
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"Moreover, overexpression of circ MTA2 significantly enhanced the interaction between UCHL3 and MTA2 ( xref E) and increased the ubiquitination level of MTA2 ( xref F)."
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"UCHL3 not only interacts with MTA2 and deubiquitinates MTA2, but also binds to CircMTA2."
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