Abstract:
:The retinoblastoma gene product (the RB protein) is phosphorylated in a cell cycle-dependent manner and this modification is believed to be important for cells to progress through the cell cycle. We found that purified cdk2 (cyclin-dependent kinase/cell division kinase 2) can phosphorylate the RB protein in vitro at the sites phosphorylated in the cell. The timing of activation of cdk2 in the cell cycle was similar to that of the onset of phosphorylation of the RB protein. The kinase coprecipitated with the RB protein also exhibited a similar substrate specificity to cdk2 and a similar time course of activation during the cell cycle. We further showed that cdk2 formed a complex with the RB protein in vitro and that its formation was not competitively inhibited by the simian virus 40 large T antigen. These observations suggest that cdk2 or a cdk2-related protein is involved in the cell cycle-dependent phosphorylation of the RB protein.
journal_name
Proc Natl Acad Sci U S Aauthors
Akiyama T,Ohuchi T,Sumida S,Matsumoto K,Toyoshima Kdoi
10.1073/pnas.89.17.7900keywords:
subject
Has Abstractpub_date
1992-09-01 00:00:00pages
7900-4issue
17eissn
0027-8424issn
1091-6490journal_volume
89pub_type
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