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Article

Mutations at multiple CDK phosphorylation consensus sites on Cdt2 increase the affinity of CRL4Cdt2 for PCNA and its ubiquitination activity in S phase.

Genes to cells : devoted to molecular & cellular mechanisms - 1 Mar 2018

Nukina Kohei, Hayashi Akiyo, Shiomi Yasushi, Sugasawa Kaoru, Ohtsubo Motoaki, Nishitani Hideo

Abstract excerpt

CRL4Cdt2 ubiquitin ligase plays an important role maintaining genome integrity during the cell cycle. A recent report suggested that Cdk1 negatively regulates CRL4Cdt2 activity through phosphorylation of its receptor, Cdt2, but the involvement of phosphorylation remains unclear. To address this, we mutated all CDK consensus phosphorylation sites located in the C-terminal half region of Cdt2 (Cdt2-18A) and...

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PMID: 29424068
DOI: 10.1111/gtc.12563

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PCNA

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Mutations at multiple CDK phosphorylation consensus sites on Cdt2 increase the affinity of CRL4Cdt2 for PCNA and its ubiquitination activity in S phase.PMID 29424068Read ↗

Cyclin-dependent kinases phosphorylate human Cdt1 and induce its degradation.Semantic proximity Read ↗

CRL4Cdt2 E3 ubiquitin ligase and proliferating cell nuclear antigen (PCNA) cooperate to degrade thymine DNA glycosylase in S phase.Semantic proximity Read ↗

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Degradation of Cdt1 during S phase is Skp2-independent and is required for efficient progression of mammalian cells through S phase.Semantic proximity Read ↗

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