An N-terminal transformation-governing sequence of SV40 large T antigen contributes to the binding of both p110Rb and a second cellular protein, p120
ME Ewen, JW Ludlow, E Marsilio, JA DeCaprio… - Cell, 1989 - cell.com
ME Ewen, JW Ludlow, E Marsilio, JA DeCaprio, RC Millikan, SH Cheng, E Paucha…
Cell, 1989•cell.comIn addition to Rb and~ 53, a third cellular protein,~ 120 in monkey and~ 118 in human cells,
forms a specific complex with SV40 large T antigen (T). p118/120 is not a product of the Rb
gene. As was shown with TlRb complex formation, the interaction between T and~ 120 is
dependent on the intact nature of a ten residue, transformation-controlling domain in T
(residues 105-114). In mouse cells, a readily detectable protein of 115 kd was detected,
which, like murfne Rb, also forms a stable complex with T. Like p118/120,~ 115 binding is …
forms a specific complex with SV40 large T antigen (T). p118/120 is not a product of the Rb
gene. As was shown with TlRb complex formation, the interaction between T and~ 120 is
dependent on the intact nature of a ten residue, transformation-controlling domain in T
(residues 105-114). In mouse cells, a readily detectable protein of 115 kd was detected,
which, like murfne Rb, also forms a stable complex with T. Like p118/120,~ 115 binding is …
Summary
In addition to Rb and~ 53, a third cellular protein,~ 120 in monkey and~ 118 in human cells, forms a specific complex with SV40 large T antigen (T). p118/120 is not a product of the Rb gene. As was shown with TlRb complex formation, the interaction between T and~ 120 is dependent on the intact nature of a ten residue, transformation-controlling domain in T (residues 105-114). In mouse cells, a readily detectable protein of 115 kd was detected, which, like murfne Rb, also forms a stable complex with T. Like p118/120,~ 115 binding is also dependent on the intact nature of the 105-114 sequence. Given their similar size and T antigen binding sequence dependence,~ 115 and p118/120 may be products of the same gene in different species. These results suggest that interactions between T and p115/118/120, as well as T and Rb, contribute to the SV40 transforming mechanism.
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