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G proteins

The arginine finger strikes again

Nature volume 389, pages 673–674 (1997)Cite this article

The Ras protein and members of its family are G (guanine-nucleotide-binding) proteins, or GTPase enzymes, that play pivotal roles in transmitting regulatory signals between the cell surface and the nucleus. Ras itself, for instance, is involved in control of cell proliferation and differentiation. These proteins are turned on by binding GTP, and off when the GTP is hydrolysed to GDP by GTPase-activating proteins, or GAPs. But how does this crucial turn-off mechanism work?

Now we know, thanks to reports1,2,3 of the three-dimensional structures of Ras and two other GTPases, crystallized in the grips of different GAPs. The crystals reveal elegantly crafted examples of convergent evolution — three structurally distinct protein machines that use identical mechanisms to promote GTP hydrolysis. Details of the structures also point to hitherto unknown regulatory functions for GAP-related switches, and they show, at atomic resolution, why Ras mutations cause 25 per cent of human cancers.

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Authors and Affiliations

  1. the Department of Cellular and Molecular Pharmacology, University of California, San Francisco, 94143, California, USA

    Henry R. Bourne

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  1. Henry R. Bourne
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Bourne, H. The arginine finger strikes again. Nature 389, 673–674 (1997). https://doi.org/10.1038/39470

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