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CDK2 phosphorylates USP37. 15 / 15
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"We found this interesting because USP37 has been implicated in cell proliferation and transformation [6, 7] as well as in cell-cycle regulation, where during the G1/S transition, CDK2 phosphorylates a[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"CDK2 regulates ERK1/2 stability by phosphorylating and activating USP37."
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"USP37 is phosphorylated by CDK2 during the G1/S-phase transition (151)."
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"Mechanistically, CDK2 phosphorylates USP37, which is required for USP37 DUB activity."
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"Cyclin A accumulation activates CDK2, which also phosphorylates USP37 to positively reinforce its catalytic activity."
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"We found this interesting because USP37 has been implicated in cell proliferation and transformation [ 6, 7 ] as well as in cell-cycle regulation, where during the G1/S transition, CDK2 phosphorylates[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"USP37, which is no longer phosphorylated by CDK2, switches from an antagonist to a substrate of APC CDH1 and is modified with degradative K11 linked polyubiquitin."
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"Meanwhile, USP37 is phosphorylated and activated by CDK2, promoting the removal of polyubiquitin chains from ERK1/2 and resulting in the stabilization of ERK1/2.USP37 promotes cancer cell growth via ERK1/2 in vitro and in vivo."
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"USP37, which is no longer phosphorylated by CDK2, switches from an antagonist to a substrate of APC CDH1 and is modified with degradative K11-linked polyubiquitin ( Figure 6 )."
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"Subsequent phosphorylation of USP37 by either CDK2 and cyclin E or CDK2 and cyclin A triggers its full DUB activity."
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"The APC-CDH1 complex does not recognize USP37 as a substrate during S/G2, possibly due to phosphorylation of USP37 by cyclin-dependent kinase 2 (CDK2)/cyclin A. Deubiquitination and phosphorylation of CDH1 by CDKs dissociates CDH1 from the core APC complex during S/G2."
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"Cyclin A accumulation activates CDK2, which also phosphorylates USP37 to positively reinforce its catalytic activity."
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"A mutation in the KEN box degron site affects the stability of USP37 and its ability to deubiquitinate cyclin A. The APC-CDH1 complex does not recognize USP37 as a substrate during S/G2, possibly due to phosphorylation of USP37 by cyclin-dependent kinase 2 (CDK2)/cyclin A. Deubiquitination and phosphorylation of CDH1 by CDKs dissociates CDH1 from the core APC complex during S/G2."
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"USP37 was inactive in mitosis because it was no longer phosphorylated by CDK2."
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"Phosphorylation of USP37 by CDK2 stimulated its full activity."
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