The INDRA Database

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"Here, we demonstrate that the deubiquitinating enzyme USP37 interacts with BLM and that USP37 deubiquitinates and stabilizes BLM, thereby sustaining the DNA damage response (DDR)."

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"Mechanistically, DNA double-strand breaks (DSB) promotes ATM phosphorylation of USP37 and enhances the binding between USP37 and BLM."

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"Mechanistically, USP37 is phosphorylated by ATM following DNA damage, which increases the binding between USP37 and BLM and leads to BLM deubiquitylation."

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"We found that only HA-tagged USP37 bound with endogenous BLM (Figure 1A)."

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"In addition, we examined the endogenous interaction between USP37 and BLM in HEK293T cells and confirmed that USP37 interacted with BLM (Figure 1C, D)."

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"To support this notion, we found that the interaction between USP37 and BLM was enhanced upon cisplatin treatment in cells (Figure 4D)."

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"Collectively, these results indicate that DNA damage can strengthen the interaction between USP37 and BLM, which in turn stabilizes BLM."

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"We found that S114A mutation attenuated the interaction between USP37 and BLM (Figure 5E)."