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#CDK1

2 public questions tagged with this topic.

Which enzyme removes inhibitory phosphate from CDK1 to activate mitosis?

Release from Wee1-mediated inhibition is pivotal for mitotic entry, executed by Cdc25 family of dual specificity phosphatases capable of hydrolyzing phospho-threonine, phospho-serine and phospho-tyrosine. Three isoforms A, B, C exist in mammals, each with N-terminal regulatory domain containing 14-3-3 binding sites, nuclear export signals, Polo box binding motifs, and C-terminal catalytic domain bearing HCX5R active site with catalytic cysteine. During unperturbed cycle Cdc25B initiates activation at centrosomes early G2, followed by Cdc25C amplifying response. Polo-like kinase 1 phosphorylate

Ref: Nilsson & Hoffmann, Cdc25 Phosphatases Activate CDK1 for Mitosis, Cell Cycle 2000; Alberts et al., Chapter 17, Cdc25 Function.

The M-phase regulator known as MPF (Maturation Promoting Factor) consists of:

Experiments in amphibian oocytes and in yeast genetics converged upon identification of universal M-phase regulator historically called Maturation Promoting Factor for its ability to induce meiotic maturation when cytoplasm from M-phase cells injected into G2 oocytes. Molecular composition resolved as complex of catalytic subunit CDK1 originally named cdc2 or p34cdc2 and regulatory subunit Cyclin B. CDK1 provides serine-threonine kinase activity requiring activating phosphorylation on activation loop Thr161 by CAK complex CDK7-Cyclin H-MAT1 and removal of inhibitory phosphates Thr14 Tyr15 via

Ref: Nurse, Universal Control of Cell Division by CDK1-Cyclin B MPF, Nature 1990; Alberts et al., Molecular Biology of the Cell, Chapter 17, Discovery of MPF.