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Insulin-Activated Phosphorylation on Tyrosine of a 15 Kilodalton Cytosolic Protein in 3T3-L1 Adipocytes

  • Michel Bernier
  • Susan C. Frost
  • Don M. Laird
  • Ronald A. Kohanski
  • M. Daniel Lane

Abstract

The action of insulin is initiated by its interaction with the insulin receptor located on the surface of target cells (1). This interaction generates a signal, which when transmitted across the plasma membrane, is propagated and distributed to pleitropic control points of cellular metabolism. Modulation by insulin of flux through these controlled reactions is responsible for regulation of the major energy storage pathways in many cell types. In the adipocyte, glucose uptake, glycogenesis and lipogenesis are accelerated by insulin.

Keywords

Insulin Receptor Phosphoamino Acid Tyrosyl Residue Phenyl Arsine Trivalent Arsenical 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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References

  1. 1.
    Lane, M.D., Life-Cycle and Regulation of the Insulin Receptor, in: “Insulin: Its Receptor and Diabetes,” M.D. Hollenberg, ed., Marcel Dekker, Inc., New York, pp. 237–264 (1985).Google Scholar
  2. 2.
    Bernier, M., Laird, D. and Lane, M.D., Proc. Natl. Acad. Sci., USA, In Press (1986).Google Scholar
  3. 3.
    Green, H. and Kehinde, 0., Cell 1: 113–116 (1974).CrossRefGoogle Scholar
  4. 4.
    Green, H. and Meuth, M., Cell, 3: 127–133 (1974).Google Scholar
  5. 5.
    Novikoff, A., Novikoff, P., Rosen, 0., and Rubin, C., J. Cell Biol. 87: 180–196 (1980).PubMedCrossRefGoogle Scholar
  6. 6.
    Mackall, J.C., Student, A.K., Polakis, S.E. and Lane, M.D., J. Biol. Chem. 251: 6462–6464 (1976).PubMedGoogle Scholar
  7. 7.
    Mackall, J.C. and Lane, M.D. Biochem. Biophys. Res. Communs. 79: 720–725 (1977).CrossRefGoogle Scholar
  8. 8.
    Coleman, R.A., Reed, B.C., Mackall, J.C., Student, A.K., Lane, M.D. and Bell, R.M., J. Biol. Chem. 253: 7256–7261 (1978).PubMedGoogle Scholar
  9. 9.
    Student, A.K., Hsu, R.Y., and Lane, M.D.,J. Biol. Chem. 255: 4745–4750 (1980).PubMedGoogle Scholar
  10. 10.
    Reed, B.C., Ronnett, G.V., Clements, P.R. and Lane, M.D. J. Biol. Chem. 256: 3917–3925 (1981).Google Scholar
  11. 11.
    Bernlohr, D.A., Angus, C.W., Lane, M.D., Bolanowski, M.A., and Kelly, Jr., T.J., Proc. Natl. Acad. Sci., USA 81: 5468–5472 (1984).CrossRefGoogle Scholar
  12. 12.
    Frost, S.C. and Lane, M.D., J. Biol. Chem. 260: 2646–2652 (1985).PubMedGoogle Scholar
  13. 13.
    Bernlohr, D.A., Bowlanowski, M.A., Kelly, Jr., T.J. and Lane, M.D., J. Biol. Chem. 260: 5563–5567 (1985).PubMedGoogle Scholar
  14. 14.
    Kohanski, R.A., Frost, S.C., and Lane, M.D., J. Biol. Chem., 261, 12272–12281 (1986).PubMedGoogle Scholar
  15. 15.
    Webb, J.L., Enzyme and Metabolic Inhibitors, Vol. III, pp. 595–793, Academic Press, New York,1966.Google Scholar
  16. 16.
    Kohanski, R.A. and Lane, M.D., Biochem. Biophys. Res. Communs. 134: 1312–1318 (1986).CrossRefGoogle Scholar
  17. 17.
    Kohanski, R.A. and Lane, M.D., J. Biol. Chem. 260: 5014–5025 (1985).PubMedGoogle Scholar
  18. 18.
    Jacobs, S., Kull, F.C.,Jr. Earp, H.S., Svoboda,M.E., Van Wyck, J.J. and Cuatrecasas, P., J. Biol. Chem. 258: 9581–9584 (1983).Google Scholar
  19. 19.
    Cohen, S., Carpenter, G., and King, L.E., Jr., J. Biol. Chem. 255: 4834–4841 (1980).PubMedGoogle Scholar
  20. 20.
    Bishayee, S., Ross, A.H., Womer, R., and Scher, C.D. Proc. Natl.Acad. Sci, USA 83: 6756–6760 (1986).PubMedCrossRefGoogle Scholar
  21. 21.
    Bernier, M., Laird, D.M., and Lane, M.D. (1987) submitted for publication.Google Scholar
  22. 22.
    Laird, D.M., Bernier, M., and Lane, M.D. (1987) submitted for publication.Google Scholar
  23. 23.
    Frost, S.C., Kohanski, R.A. and Lane, M.D. (1987) submitted for publication.Google Scholar
  24. 24.
    Tamura, S., Brown, T.A., Whipple, J.H., Fujita-Yamaguchi, Y., Dublers, R.E., Cheng, K. and Larner, J., J. Biol. Chem. 259: 6650–6658 (1984).PubMedGoogle Scholar
  25. 25.
    Dubyak, G.R. and Kleinzeller, A. J. Biol. Chem. 255: 5306–5312 (1980).Google Scholar

Copyright information

© Plenum Press, New York 1987

Authors and Affiliations

  • Michel Bernier
    • 1
  • Susan C. Frost
    • 1
  • Don M. Laird
    • 1
  • Ronald A. Kohanski
    • 1
  • M. Daniel Lane
    • 1
  1. 1.Department of Biological ChemistryThe Johns Hopkins University School of MedicineBaltimoreUSA

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