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"We subsequently confirmed that USP15 could bind to ATM both endogenously and exogenously via confocal microscopy, dual-link proximity ligation assay (PLA), and reciprocal coimmunoprecipitation (Co-IP) experiments (Fig. 4b–e)."

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"Therefore, the direct binding between USP15 and ATM is deubiquitination independent."

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"Next, we tested which region of USP15 is responsible for its interaction with ATM by expressing ATM together with USP15 or its truncated mutants (Fig. 4h) and found that the USP15 D3 deletion mutant (deletion residues 740–981) abolished the binding of USP15 with ATM (Fig. 4i)."