IndraLab

Statements

CDK1 binds USP37. 11 / 11
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"In summary, these results indicate that these human CRC data align well with our experimental findings regarding the CDK1–USP37 axis-mediated stability of SND1 and the proliferation and invasion-metastasis of CRC cells, and that dysregulation of the CDK1–USP37–SND1 axis leads to poor prognosis in CRC ( xref J)."
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"To confirm the interaction between endogenous USP37 and CDK1, we conducted co-IP experiments."
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"We found that CDK1 binds to USP37 and phosphorylates it at Thr631, with the phosphorylation-deficient mutant almost entirely losing its functionality, highlighting the critical nature of these phosphorylation events for USP37 activity targeting SND1."
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"In this study, we unveiled the crucial role of the CDK1–USP37 axis in stabilizing SND1 and its oncogenic functions, proposing therapeutic strategies targeting this axis, and potentially offering new insights and treatment approaches to combat CRC proliferation and metastasis."
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"This study not only elucidated the regulatory mechanism of the CDK1–USP37 axis involved in the stability of SND1, but also found that dacarbazine is a potent inhibitor of USP37 and a promising candidate for the treatment of CRC."
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"Notably, the preclinical evidence we provided strongly suggests that targeting the CDK1–USP37 axis can effectively disrupt the stability of SND1, thereby inhibiting cancer cell proliferation and tumor metastasis in CRC."
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"To further verify the interaction between exogenous USP37 and CDK1, cells were transfected to express Flag-CDK1 and HA-USP37, followed by co-IP with anti-HA or FLAG antibodies."
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"Future studies should also investigate potential compensatory pathways that may be activated when the CDK1–USP37 axis is inhibited."
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"Moreover, purified GST-USP37, but not GST alone, interacted with Flag-CDK1 in vitro , demonstrating a direct interaction between USP37 and CDK1 ( xref E)."
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"These results definitively indicate that exogenous USP37 could bind to exogenous CDK1 ( xref )."
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"CDK1 binds and phosphorylates USP37."
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