Abstract:
:The product of the retinoblastoma susceptibility gene, pRB, is a nuclear phosphoprotein that controls cell growth by binding to and suppressing the activities of transcription factors such as the E2F family. Transactivation activity is inhibited when E2F is bound to hypophosphorylated pRB and released when pRB is phosphorylated by cyclin-dependent kinases (CDKs). To determine which of 16 potential CDK phosphorylation sites regulated the pRB-E2F interaction, mutant pRB proteins produced by site-directed mutagenesis were tested for the ability to suppress E2F-mediated transcription in a reporter chloramphenicol acetyltransferase assay. Surprisingly, no one CDK site regulated the interaction of pRB with E2F when E2F was bound to DNA. Instead, disruption of transcriptional repression resulted from accumulation of phosphate groups on the RB molecule.
journal_name
Mol Cell Bioljournal_title
Molecular and cellular biologyauthors
Brown VD,Phillips RA,Gallie BLdoi
10.1128/mcb.19.5.3246subject
Has Abstractpub_date
1999-05-01 00:00:00pages
3246-56issue
5eissn
0270-7306issn
1098-5549journal_volume
19pub_type
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