CDKG1 is a D-cyclin dependent retinoblastoma related protein kinase whose abundance scales with cell size and controls cell division cycle number during multiple fission.
Cyclin-dependentkinase 2 (Cdk2), the master regulator of S phase events during the cell cycle, controls the earliest step in the motile ciliogenesis pathway in quiescent multiciliatedairway epithelial cells.
A new tumor suppressor function of p21, needed at each undamaged duplication cycle, ensures the adequate execution of the DNA replication program thereby protecting the genome integrity.
CDPK4 is a pleiotropic regulator controlling initiation of DNA replication, mitotic spindle assembly and flagellar activation during the early stages of Plasmodium transmission.
Ablation of the Cdkn1c cell cycle inhibitor leads to defective muscle stem cell dynamics and myogenic potential, while progressive cytoplasmic to nuclear cellular localization of the Cdkn1c protein regulates growth arrest.
By distributing regulation to both the GTPase and downstream kinases, the Mitotic Exit Network creates a single signal from spatial and temporal inputs.
Quantitative phosphoproteomics defines the substrates for Cyclin A/Cdk1 kinase during early mitosis and follow up studies validate that one identified substrate, MYPT1, influences the stability of k-MT attachments by regulating Plk1.
Reconstructing ancestral enzymes has revealed that a switch in kinase substrate preference evolved via an expanded specificity intermediate that is tolerated in vivo, thus providing a path for kinase diversification.
