Abstract:
:The growth-suppressive activity of the retinoblastoma (RB) protein is suggested to be regulated by phosphorylation. In studies on the kinase that phosphorylates the RB proteins, we have previously found that RB proteins can be phosphorylated by purified cdc2 kinase. In this study, we noted that RB proteins immunoprecipitated from human cell lysates are weakly phosphorylated in the absence of purified cdc2 kinase. Immunoblot analysis showed the presence of p34cdc2 in the immunoprecipitates with anti-RB monoclonal antibody. In addition, the coprecipitated kinase was found to have the same substrate specificity as cdc2 kinase. The associated kinase activity was particularly high in cells arrested in G1/S and S phase by aphidicolin. Furthermore, RB proteins were shown to be phosphorylated in nuclear extracts by some endogenous cdc2-like kinase(s). These results suggest that cdc2-like kinase is the main kinase for phosphorylation of RB proteins in vivo.
journal_name
Oncogenejournal_title
Oncogeneauthors
Kitagawa M,Saitoh S,Ogino H,Okabe T,Matsumoto H,Okuyama A,Tamai K,Ohba Y,Yasuda H,Nishimura Ssubject
Has Abstract,Author List Incompletepub_date
1992-06-01 00:00:00pages
1067-74issue
6eissn
0950-9232issn
1476-5594journal_volume
7pub_type
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