Polyoma middle tumor antigen interacts with SHC protein via the NPTY (Asn-Pro-Thr-Tyr) motif in middle tumor antigen

Kathryn S. Campbell, Egon Ogris, Brenda Burke, Wen Su, Kurt R. Auger, Brian Druker, Brian S. Schaffhausen, Thomas M. Roberts, David C. Pallas

Research output: Contribution to journalArticle

141 Citations (Scopus)

Abstract

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-ProThr-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.

Original languageEnglish (US)
Pages (from-to)6344-6348
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume91
Issue number14
StatePublished - Jul 5 1994

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Neoplasm Antigens
Phosphatidylinositol 3-Kinase
Proteins
Polyomavirus Transforming Antigens
src-Family Kinases
Tyrosine
Phosphotransferases
Cell Count

ASJC Scopus subject areas

  • General
  • Genetics

Cite this

Polyoma middle tumor antigen interacts with SHC protein via the NPTY (Asn-Pro-Thr-Tyr) motif in middle tumor antigen. / Campbell, Kathryn S.; Ogris, Egon; Burke, Brenda; Su, Wen; Auger, Kurt R.; Druker, Brian; Schaffhausen, Brian S.; Roberts, Thomas M.; Pallas, David C.

In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 91, No. 14, 05.07.1994, p. 6344-6348.

Research output: Contribution to journalArticle

Campbell, KS, Ogris, E, Burke, B, Su, W, Auger, KR, Druker, B, Schaffhausen, BS, Roberts, TM & Pallas, DC 1994, 'Polyoma middle tumor antigen interacts with SHC protein via the NPTY (Asn-Pro-Thr-Tyr) motif in middle tumor antigen', Proceedings of the National Academy of Sciences of the United States of America, vol. 91, no. 14, pp. 6344-6348.
Campbell, Kathryn S. ; Ogris, Egon ; Burke, Brenda ; Su, Wen ; Auger, Kurt R. ; Druker, Brian ; Schaffhausen, Brian S. ; Roberts, Thomas M. ; Pallas, David C. / Polyoma middle tumor antigen interacts with SHC protein via the NPTY (Asn-Pro-Thr-Tyr) motif in middle tumor antigen. In: Proceedings of the National Academy of Sciences of the United States of America. 1994 ; Vol. 91, No. 14. pp. 6344-6348.
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abstract = "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-ProThr-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.",
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AU - Auger, Kurt R.

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AB - 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-ProThr-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.

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