GITAB Knowledge Hub Biology Diagrams 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
In both, the phosphorylation is a predominant event and plays an important role in cell survival (AKT activation phosphorylates BAD and MDM2), cell proliferation (AKT activation phosphorylates FoxO, RAS phosphorylates RAF and it phosphorylates MEK that phosphorylates Erk1/2), cell migration (phosphorylation cascade of RAS), apoptosis (AKT
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Phosphorylation and the cell cycle Biology Diagrams
The cell cycle governs a precise series of molecular events, regulated by coordinated changes in protein and phosphorylation abundance, that culminates in the generation of two daughter cells. 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.
Role of Protein Phosphorylation in the Regulation of Cell Cycle and DNA ... Biology Diagrams
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 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.
