Analysis of p107-associated proteins: p107 associates with a form of E2F that differs from pRB-associated E2F-1

N Dyson, M Dembski, A Fattaey, C Ngwu… - Journal of …, 1993 - Am Soc Microbiol
N Dyson, M Dembski, A Fattaey, C Ngwu, M Ewen, K Helin
Journal of virology, 1993Am Soc Microbiol
The binding of viral oncogenes to cellular proteins is thought to modulate the activities of
these cellular targets. The p107 protein is targeted by many viral proteins, including
adenovirus E1A, simian virus 40 large T antigen, and human papillomavirus type 16 E7
protein. A panel of monoclonal antibodies against p107 was raised and used to identify
cellular proteins that interact with the p107 protein in vivo. p107-associated proteins
included cyclin A, cyclin E, and cdk2. In addition, p107 was found to associate with 62-to 65 …
The binding of viral oncogenes to cellular proteins is thought to modulate the activities of these cellular targets. The p107 protein is targeted by many viral proteins, including adenovirus E1A, simian virus 40 large T antigen, and human papillomavirus type 16 E7 protein. A panel of monoclonal antibodies against p107 was raised and used to identify cellular proteins that interact with the p107 protein in vivo. p107-associated proteins included cyclin A, cyclin E, and cdk2. In addition, p107 was found to associate with 62- to 65- and 50-kDa phosphoproteins in ML-1 cells, a human myeloid leukemia cell line. The 62- to 65-kDa proteins have many of the properties of the transcription factor E2F but were distinguished from pRB-associated E2F-1 by both immunologic and biochemical properties.
American Society for Microbiology