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Regulation and Functions of Src-Family Kinases: An Update

  • Conference paper
Tyrosine Phosphorylation/Dephosphorylation and Downstream Signalling

Part of the book series: NATO ASI Series ((ASIH,volume 76))

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Abstract

Perhaps the most intensively studied tyrosine kinases are the products of the viral and cellular src genes. Mutations in v-src which abolish catalytic activity also prevent transformation, indicating that the tyrosine kinase activity of the viral oncoprotein p60v-src is required for its function (Martin, 1970; Sefton et al., 1980; reviewed by Jove & Hanafusa, 1987). Indeed, cells transformed by v-src show about a ten-fold increase in the phosphorylation of cellular proteins on tyrosine, compared to normal controls (Hunter & Sefton, 1980; Sefton et al., 1980; Jakobovits et al., 1984). Presumably, the tyrosine phosphorylation of certain critical substrates initiates and maintains the transformed phenotype, since shifting cells transformed by temperature-sensitive mutants of v-src to the restrictive temperature causes reversion of transformed morphology within several hours (reviewed by Jove & Hanafusa, 1987).

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  1. Fred Hutchinson Cancer Research Center, 1124 Columbia Street, Seattle, Washington, 98104, USA

    S. Kussick & J. A. Cooper

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  1. S. Kussick
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  1. Institut für Physiologische Chemie, Abteilung für Biochemie Supramolekularer Systeme, Ruhr-Universität Bochum, Medizinische Fakultät, D-44780, Bochum, Germany

    Ludwig M. G. Heilmeyer Jr.

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Kussick, S., Cooper, J.A. (1993). Regulation and Functions of Src-Family Kinases: An Update. In: Heilmeyer, L.M.G. (eds) Tyrosine Phosphorylation/Dephosphorylation and Downstream Signalling. NATO ASI Series, vol 76. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-78247-3_2

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  • DOI: https://doi.org/10.1007/978-3-642-78247-3_2

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