Reactome | Full activity of most CDKs is dependent on CAK mediated phos...

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created	[InstanceEdit:170184] Matthews, L, 2005-12-28 10:02:46
dbId	170192
displayName	Full activity of most CDKs is dependent on CAK mediated phos...
literatureReference	[LiteratureReference:77499] Effects of phosphorylation by CAK on cyclin binding by CDC2 and CDK2. [LiteratureReference:9928866] Distinct activation pathways confer cyclin-binding specificity on Cdk1 and Cdk2 in human cells [LiteratureReference:9929418] Coupling of T161 and T14 phosphorylations protects cyclin B-CDK1 from premature activation
modified	[InstanceEdit:9929419] Orlic-Milacic, Marija, 2024-11-25
schemaClass	Summation
text	Full activity of most CDKs is dependent on CAK mediated phosphorylation at a conserved residue (Thr161 in CDK1, also known as Cdc2). This modification is thought to improve substrate binding. High affinity binding of Cyclin A within the Cyclin A:Cdc2 complex requires this phosphorylation (Desai et al 1995, Merrick et al. 2008). CAK is unable to phosphorylate monomeric CDK1 and only phosphorylates it when it is bound to cyclin A or cyclin B (Merrick et al. 2008). Using two-dimensional gel electrophoresis of protein extracts of cycling human cells, it was shown that CDK1 phosphorylated at both T14 nad T161 can be co-immunoprecipitated with CCNA2 before mitosis (Coulonval et al. 2011).

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