The E2F transcription factor is a cellular target for the RB protein

Role of caspases and possible involvement of retinoblastoma protein during TGFβ-mediated apoptosis of human B lymphocytes

“…This degradation could then result in the loss of the anti-apoptotic activity associated with the non-cleaved form of Rb. Various reports suggest that the anti-apoptotic activity of Rb is preferentially expressed by the unphosphorylated form (Berry et al, 1996;Fan et al, 1996) which is the active form binding various factors including E2F-1 (Chellappan et al, 1991;Kato et al, 1993;Nevins, 1992). Thus TGFb-mediated accumulation of unphosphorylated Rb may be the ®rst step allowing further e cient caspase-mediated proteolysis of unphosphorylated Rb.…”

GOOSECOID inhibits erythrocyte differentiation by competing with Rb for PU.1 binding in murine cells

“…As interaction of Rb with other proteins has been demonstrated in a number of contexts (Chellappan et al, 1991;Dowdy et al, 1993;Gu et al, 1993;Hagemeier et al, 1993;Whyte et al, 1988), we hypothesized that a speci®c interaction might occur in F5-5 cultures upon activin treatment. F5-5 cells were cultured with or without activin and immunoprecipitated with rabbit anti-Rb antibodies or rabbit anti-CDK4 antibodies as control.…”

Identification of a p130 domain mediating interactions with cyclin A/cdk 2 and cyclin E/cdk 2 complexes

“…In almost all cases involving interactions with pRB, phosphorylation of pRB abrogates the interaction. For example, phosphorylation of pRB results in its dissociation from E2F transcription factors (Chellappan et al, 1991;Helin et al, 1992;Shan et al, 1992;Ewen et al, 1993;Dynlacht et al, 1994;Bremner et al, 1995;Suzuki-Takahashi et al, 1995) and from E1A, T antigen and E7 (Ludlow et al, 1990;Imai et al, 1991;Templeton and Weinberg, 1991). Phosphorylation of p107 appears to regulate its association with E2F proteins in a manner analogous to pRB (Bejersbergen et al, 1995;Xiao et al, 1996).…”