Autor: |
Campbell, K S, Ogris, E, Burke, B, Su, W, Auger, K R, Druker, B J, Schaffhausen, B S, Roberts, T M, Pallas, D C |
Zdroj: |
Proceedings of the National Academy of Sciences of the United States of America; July 1994, Vol. 91 Issue: 14 p6344-6348, 5p |
Abstrakt: |
Polyomavirus middle tumor antigen (MT) transforms a large number of cell types by binding to and modulating the activities of cellular proteins. Previous genetic analysis defined in MT an independent motif, NPTY (Asn-Pro-Thr-Tyr), required for transformation. This report demonstrates that NPTY is required for interaction between MT and SHC protein, a Src homology 2 (SH2)-containing protooncogene product implicated in activating Ras via association with GRB2 protein. SHC is phosphorylated on tyrosine and associates with GRB2 in MT-transformed cells. These effects require an intact NPTY motif in MT. SHC immunoprecipitates from MT-transformed cells possess kinase activity that phosphorylates not only SHC and MT but also the 85-kDa subunit of phosphatidylinositol 3-kinase. This result suggests that a complex exists that contains, at a minimum, MT, Src family tyrosine kinases, phosphatidylinositol 3-kinase, and SHC. |
Databáze: |
Supplemental Index |
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