The Role of Phosphorylation in Growth Control and Malignant Transformation

  • Tony Hunter
Conference paper
Part of the NATO ASI Series book series (NSSA, volume 135)


Experiments with cultured cells suggest that the growth of mammalian cells is regulated largely by growth factors and inhibitors acting at the G0/G1 border in cell cycle. Growth factors are mostly polypeptide in nature (e.g. EGF, PDGF, FGF, IGF-1, bombesin) and range in mass from 2,000 to 70,000 daltons. Cells responsive to a given growth factor have specific cell surface receptors, usually numbering between 103 and 106 per cell, with a high affinity (Kd 10-8 to 10-11) and specificity for their ligand. Occupancy of these receptors results in the transduction of a signal across the membrane to the cytoplasm, the nature of which will be discussed below. Bona fide growth inhibitors have only recently been purified to homogeneity (e.g. TGF-β, interferon), although their existence had been surmised for many years. Their mode of action is not understood, but, like the polypeptide growth factors, growth inhibitors have specific high affinity surface receptors, which presumably transduce signals to the cytoplasm. Another external component essential for cell growth is the extracellular matrix, comprised of proteins like fibronectin, laminin, and collagen, and the glycosaminoglycans. Adherent cells will not grow in the absence of an extracellular matrix, but most cells are capable of elaborating their own matrix. There are specific surface receptors for these matrix proteins, but it is not yet known whether the binding of ligand to this type of receptor causes a signal transduction event.


Growth Factor Receptor Tyrosine Phosphorylation Protein Kinase Activity Mitogenic Response Protein Kinase Domain 
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Copyright information

© Plenum Press, New York 1987

Authors and Affiliations

  • Tony Hunter
    • 1
  1. 1.Molecular Biology and Virology LaboratorySalk InstituteSan DiegoUSA

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