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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

Functional analysis of the P box, a domain in cyclin B required for the activation of Cdc25.

Cyclin B-cdc2 complexes are kept inactive by inhibitory phosphorylations on Thr-14 and Tyr-15 of cdc2 until they are dephosphorylated at the end of G2 by the phosphatase cdc25. Recent work has suggested that a small region of cyclin B, which we call the P box, may contribute part of a phosphatase- activating domain to cdc25. Individual conservative substitutions at three invariant residues within the P box yield mutant cyclin B proteins that bind cdc2 in vitro and then show the predicted cell cycle arrest, with cdc25 remaining in the low activity interphase form and cyclin B-cdc2 complexes remaining phosphorylated and inactive. While the low activity interphase form of cdc25 cannot act on cdc2 complexed with a mutant P box cyclin, the high activity M phase form of cdc25 can. These results demonstrate that the P box domain of cyclin B is required for cdc25 activation and support a two-step mechanism for the cdc25-dependent activation of cyclin B-cdc2.[1]


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