CCNA:CDK1 phosphorylates HJURP

Stable Identifier
R-HSA-9929884
Type
Reaction [transition]
Species
Homo sapiens
Compartment
ReviewStatus
5/5
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HJURP (Holliday junction recognition protein), a centromeric protein required for the incorporation of newly synthesized CENPA molecules into nucleosomes at replicated centromeres (Foltz et al. 2009, Dunleavy et al. 2009), was identified as a CCNA:CDK2 target in a high-throughput screen (Dumitru et al. 2017). HJURP was shown to be phosphorylated at G2, at least on two CDK consensus sites, S211 and S412, at a time that correlates with high CDK1 activity, and that it binds to CCNA2, and, to a lesser extent, to CCNB (Stankovic et al. 2017). The interaction with CCNA2 is required for the CDK-mediated inhbition of an untimely recruitment of HJURP to the centromere (Stankovic et al. 2017).
Literature References
PubMed ID Title Journal Year
28017591 A Dual Inhibitory Mechanism Sufficient to Maintain Cell-Cycle-Restricted CENP-A Assembly

Stankovic, A, Guo, LY, Mata, JF, Bodor, DL, Cao, XJ, Bailey, AO, Shabanowitz, J, Hunt, DF, Garcia, BA, Black, BE, Jansen, LET

Mol Cell 2017
29154753 Cyclin A/Cdk1 modulates Plk1 activity in prometaphase to regulate kinetochore-microtubule attachment stability

Dumitru, AMG, Rusin, SF, Clark, AEM, Kettenbach, AN, Compton, DA

Elife 2017
Participants
Participates
Catalyst Activity

cyclin-dependent protein serine/threonine kinase activity of p-S-CCNA:p-T161-CDK1 [nucleoplasm]

Orthologous Events
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