The phosphorylation process and the potential functions of Biology Diagrams We provide information regarding the phosphorylation events over the cell cycle, and a method of comparing these to protein and transcript level dynamics. Besides the post-translational regulation of protein activity, the intracellular localization plays a major role and the compartmentalization of the cell serves as a well-recognized way to
This is achieved by rising CDK activity and the differential sensitivity of substrates to CDK activity over a wide dynamic range. This is combined with rapid phosphorylation turnover to generate clearly resolved substrate-specific activity thresholds, which in turn ensures the appropriate ordering of downstream cell-cycle events. Since phosphorylation events both depend on the structural environment and influence its properties, protein structure and phosphorylation should be considered interrelated and mutually dependent. The variation of phosphorylation changes over the cell cycle scales with the structural propensities of the phosphorylated residues: from lowest
Phosphorylation Variation during the Cell Cycle Scales with ... Biology Diagrams
Cell-cycle phosphorylation is temporally ordered, at least in part, through the sequential expression of different cyclins. Recent studies by Swaffer et al. and Godfrey et al. 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.
Phosphorylation of about 75% of the protein kinases they identified was upregulated more than twofold in M phase, suggesting that cell-cycle progression involves extensive rearrangements of
CDK activity at the centrosome regulates the cell cycle Biology Diagrams
The cell cycle is a highly conserved process involving the coordinated separation of a single cell into two daughter cells. To relate transcriptional regulation across the cell cycle with oscillatory changes in protein abundance and activity, we carried out a proteome- and phospho-proteome-wide mass spectrometry profiling.
