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The ras oncogene product p21 is not a regulatory component of adenylate cyclase

Nature volume 317, pages 71–72 (1985)Cite this article

Abstract

Harvey (Ha-MSV) and Kirsten (Ki-MSV) murine sarcoma viruses induce tumours in animals and transform various cells in culture because of the expression of the ras oncogene product, p21 (ref. 1). Proto-oncogenes homologous with these genes are highly conserved evolutionarily2 and activated ras oncogenes have been detected in many human cancers3–7. Whether c-ras oncogenes are directly responsible for human carcinogenesis is uncertain; however, it is clear that p21 mediates virus-induced transformation, although by an unknown mechanism. Epithelial and fibroblast cell lines transformed with Ha-MSV and Ki-MSV express p21 (ref. 8) and exhibit reduced adenylate cyclase activity9,10. Like the guanine nucleotide regulatory proteins, Ns and Ni, which mediate stimulation11 and inhibition12, respectively, of adenylate cyclase, p21 is a membrane-associated GTP binding protein, which exhibits GTPase activity13–15. These similarities suggest that p21 and the adenylate cyclase regulatory proteins are related in cellular function, and that p21 depresses adenylate cyclase by inhibiting the activity of Ns or acting as Ni. We have therefore now examined the structural and functional similarities between p21 and Ns and Ni and find no evidence that p21 regulates adenylate cyclase activity by acting as one of these regulatory proteins.

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Author notes

  1. Seisuke Hattori and Thomas Y. Shih: Laboratory of Molecular Oncology, National Cancer Institute, National Institutes of Health, Frederick, Maryland 21701, USA

Authors and Affiliations

  1. Laboratory of Cellular and Developmental Biology, Diabetes, Digestive and Kidney Diseases, National Institute of Arthritis, Bethesda, Maryland, 20205, USA

    Suzanne K. Beckner, Seisuke Hattori & Thomas Y. Shih

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  1. Suzanne K. Beckner
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  2. Seisuke Hattori
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  3. Thomas Y. Shih
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Beckner, S., Hattori, S. & Shih, T. The ras oncogene product p21 is not a regulatory component of adenylate cyclase. Nature 317, 71–72 (1985). https://doi.org/10.1038/317071a0

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