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Specific dephosphorylation of membrane proteins in Rous sarcoma virus-transformed chick embryo fibroblasts

Naturevolume 287pages241244 (1980) | Download Citation

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Abstract

Chick embryo fibroblasts (CEF) infected with avian sarcoma virus become rapidly transformed as a result of expression of the viral src gene1,2 in the form of a single polypeptide of molecular weight 60,000 (pp60src)3 with protein kinase activity4 and suggested preferential association with the plasma membrane5,6. Studies with normal avian and mammalian cells have revealed the presence of an antigenically related protein7,8 which seems to have similar kinase activity, but which is present at less than 1% of the levels of virally induced src protein found in transformed cells8,9. As dynamic protein phosphorylation is important in numerous regulatory processes10,11, the phenotypic expression of transformation may arise from an imbalance in one or more regulatory mechanisms that are controlled by protein phosphorylation4,8,12. The cell membrane is affected during transformation13, including its phosphotransferase activity14,15. The latter has been shown using isolated membrane fractions whose properties may be changed during preparation16. Therefore, we have compared the phosphorylation state of individual membrane proteins found in intact normal and RSV-transformed cells and report here the identification of two heavily phosphorylated, acidic membrane proteins in normal CEF which are specifically dephosphorylated on transformation by wild-type and temperature-sensitive Rous sarcoma viruses.

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Affiliations

  1. Department of Pathology, University of Colorado Health Sciences Center, Denver, Colorado, 80262

    • Daniel P. Witt
    •  & Julius A. Gordon

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https://doi.org/10.1038/287241a0

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