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Mol. Cell. Biol., Jan 1995, 345-350, Vol 15, No. 1
Copyright © 1995, American Society for Microbiology

Effects of phosphorylation by CAK on cyclin binding by CDC2 and CDK2

D Desai, HC Wessling, RP Fisher and DO Morgan
Department of Physiology, University of California, San Francisco 94143- 0444.

The cyclin-dependent protein kinases (CDKs) are activated by association with cyclins and by phosphorylation at a conserved threonine residue by the CDK-activating kinase (CAK). We have studied the binding of various human CDK and cyclin subunits in vitro, using purified proteins derived from baculovirus-infected insect cells. We find that most CDK-cyclin complexes known to exist in human cells (CDC2- cyclin B, CDK2-cyclin A, and CDK2-cyclin E) form with high affinity in the absence of phosphorylation or other cellular components. One complex (CDC2-cyclin A) forms with high affinity only after CAK- mediated phosphorylation of CDC2 at the activating threonine residue. CDC2 does not bind with high affinity to cyclin E in vitro, even after phosphorylation of the CDC2 subunit. Thus, phosphorylation is of varying importance in the formation of high-affinity CDK-cyclin complexes.


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