Cdks and the Drosophila cell cycle
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Cited by (28)
CDK phosphorylation inhibits the DNA-binding and ATP-hydrolysis activities of the Drosophila origin recognition complex
2005, Journal of Biological ChemistryCitation Excerpt :Although Cdk phosphorylation sites are not strictly conserved between yeast, Drosophila, Xenopus, and mammals, the relative arrangement of potential Cdk sites in subunits Orc1p and Orc2p is similar in all eukaryotes, suggesting that control of the ATPase activity of ORC through Cdk phosphorylation may be conserved in other eukaryotes (supplemental Fig. S5). Inhibition of the ability of DmORC to bind to DNA in an ATP-bound state provides an obvious mechanism by which Cdks could exert re-replication control in vivo and would be consistent with the requirement for alternating Cdk2·cyclin E activity during Drosophila endocycles and alternating Cdk activity during normal mitotic cycles (60–62). The ORCs from all species studied to date can bind to DNA in an ATP-independent mode, but for ScORC and DmORC the ATP-dependent interaction shows higher affinity.
When timing is everything: Role of cell cycle regulation in asymmetric division
2005, Seminars in Cell and Developmental BiologyCitation Excerpt :Like in other eukaryotes, the decision to enter mitosis during embryonic cell cycles in Drosophila is governed largely by Cdc2/Cdk1 phosphorylation state and by levels of mitotic cyclins (reviewed in [12–14]).
Control of endoreduplication domains in the Drosophila gut by the knirps and knirps-related genes
2001, Mechanisms of DevelopmentEstablishing links between developmental signaling pathways and cell-cycle regulation in Drosophila
1999, Current Opinion in Genetics and Development