The Temporal Ordering of Cell-Cycle Phosphorylation.
Cell-cycle phosphorylation is temporally ordered, at least in part, through the sequential expression of different cyclins. Recent studies by Swaffer et al. (2016) and Godfrey et al. (2017) show that intrinsic properties of the substrate proteins contribute as well: good kinase substrates tend to be phosphorylated early, and good phosphatase substrates tend to be phosphorylated late.
Department of Chemical and Systems Biology, Stanford University School of Medicine, Stanford, CA 94305-5174, USA.
Julia
J
Kamenz
Department of Chemical and Systems Biology, Stanford University School of Medicine, Stanford, CA 94305-5174, USA; Department of Biochemistry, Stanford University School of Medicine, Stanford, CA 94305-5307, USA. Electronic address: james.ferrell@stanford.edu.
James E
JE
Ferrell
D000818:Animals; D002453:Cell Cycle; D018797:Cell Cycle Proteins / Q000378:metabolism; D018844:Cyclin-Dependent Kinases / Q000378:metabolism*; D016213:Cyclins / Q000378:metabolism*; D005656:Fungal Proteins / Q000378:metabolism; D005786:Gene Expression Regulation; D006801:Humans; D008024:Ligands; D010744:Phosphoric Monoester Hydrolases / Q000378:metabolism*; D010766:Phosphorylation; D013379:Substrate Specificity
D018797:Cell Cycle Proteins; D016213:Cyclins; D005656:Fungal Proteins; D008024:Ligands; D018844:Cyclin-Dependent Kinases; D010744:Phosphoric Monoester Hydrolases