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Signal transduction

New exchange, new target

Nature volume 396, pages 416–417 (1998)Cite this article

The Ras superfamily of small guanine-nucleotide-binding (G) proteins controls many aspects of cellular behaviour, from proliferation and survival to morphology and membrane transport. Despite their varied effects, these proteins are regulated by a common mechanism — the opposing effects of stimulatory guanine-nucleotide-exchange factors (GEFs), which promote the uptake of fresh GTP to form an active, GTP-bound conformation, and inhibitory guanosine triphosphatase activating proteins, which stimulate hydrolysis of bound GTP to form the inactive, GDP-bound conformation.

On page 474 of this issue, de Rooij et al.1 report a new twist to the mechanism for control of the Ras-related protein Rap1. Their study shows that regulation of proteins in the Ras superfamily is considerably more varied than previously thought, and establishes, for the first time, the molecular details of how a Ras-related protein is controlled. As well as all this, the authors identify a new class of target protein for cyclic AMP, Earl Sutherland's original second messenger molecule, raising the possibility that several of cAMP's effects on cells may not be mediated by its previously characterized targets.

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Figure 1: Two types of regulatory system for Ras proteins.

References

  1. de Rooij, J. et al. Nature 396, 474–477 (1998).

    Article  ADS  CAS  Google Scholar 

  2. McCormick, F. Nature 363, 15–16 (1993).

    Article  ADS  CAS  Google Scholar 

  3. Farnsworth, C. L. et al. Nature 376, 524–527 (1995).

    Article  ADS  CAS  Google Scholar 

  4. Mattingly, R. R. & Macara, I. G. Nature 382, 268–272 (1996).

    Article  ADS  CAS  Google Scholar 

  5. Ebinu, J. O. et al. Science 280, 1082–1086 (1998).

    Google Scholar 

  6. Kitayama, H., Sugimoto, Y., Matsuzaki, T., Ikawa, Y. & Noda, M. Cell 56, 77–84 (1989).

    Google Scholar 

  7. Bos, J. L. EMBO J. 17, 6776–6782 (1998).

    Google Scholar 

  8. Zwartkruis, F. J., Wolthuis, R. M., Nabben, N. M., Franke, B. & Bos, J. L. EMBO J. 17, 5905–5912 (1998).

    Google Scholar 

  9. York, R. D. et al. Nature 392, 622–626 (1998).

    Article  ADS  CAS  Google Scholar 

  10. Altschuler, D. L., Peterson, S. N., Ostrowski, M. C. & Lapetina, E. G. J. Biol. Chem. 270, 10373–10376 (1995).

    Google Scholar 

  11. Franke, B., Akkerman, J. W. & Bos, J. L. EMBO J. 16, 252–259 (1997).

    Google Scholar 

Download references

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Authors and Affiliations

  1. the Signal Transduction Laboratory, Imperial Cancer Research Fund, 44 Lincolns Inn Fields, London, WC2A 3PX, UK

    Julian Downward

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  1. Julian Downward
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Downward, J. New exchange, new target. Nature 396, 416–417 (1998). https://doi.org/10.1038/24743

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