Differential regulation of retinoblastoma protein function by specific Cdk phosphorylation sites
ES Knudsen, JYJ Wang - Journal of Biological Chemistry, 1996 - ASBMB
The retinoblastoma tumor suppressor protein, RB, contains at least three distinct protein
binding domains. The A/B pocket binds proteins with the LXCXE motif, the C pocket binds
the nuclear c-Abl tyrosine kinase, and the large A/B pocket binds the transcription factor E2F.
Dissociation of RB from its targets is observed as RB becomes phosphorylated during G 1/S
progression. There are 16 Cdk consensus phosphorylation sites in RB. It was previously
unknown whether the many phosphorylation sites had redundant or distinct functions in the …
binding domains. The A/B pocket binds proteins with the LXCXE motif, the C pocket binds
the nuclear c-Abl tyrosine kinase, and the large A/B pocket binds the transcription factor E2F.
Dissociation of RB from its targets is observed as RB becomes phosphorylated during G 1/S
progression. There are 16 Cdk consensus phosphorylation sites in RB. It was previously
unknown whether the many phosphorylation sites had redundant or distinct functions in the …
