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It takes two to tango: regulation of G proteins by dimerization

Nature Reviews Molecular Cell Biology volume 10, pages 423–429 (2009)Cite this article

Abstract

Guanine nucleotide-binding (G) proteins, which cycle between a GDP- and a GTP-bound conformation, are conventionally regulated by GTPase-activating proteins (GAPs) and guanine nucleotide-exchange factors (GEFs), and function by interacting with effector proteins in the GTP-bound 'on' state. Here we present another class of G proteins that are regulated by homodimerization, which we would categorize as G proteins activated by nucleotide-dependent dimerization (GADs). This class includes proteins such as signal recognition particle (SRP), dynamin, septins and the newly discovered Roco protein Leu-rich repeat kinase 2 (LRRK2). We propose that the juxtaposition of the G domains of two monomers across the GTP-binding sites activates the biological function of these proteins and the GTPase reaction.

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Figure 1: Two versions of the GTPase cycle.
Figure 2: Structures of G proteins activated by nucleotide-dependent dimerization
Figure 3: The G protein cycle of GADs.

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  1. Abteilung Strukturelle Biologie, Max-Planck-Institut für Molekulare Physiologie, Otto-Hahn Strasse 11, Dortmund, 44227, Germany

    Raphael Gasper, Simon Meyer, Katja Gotthardt, Minhajuddin Sirajuddin & Alfred Wittinghofer

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  1. Raphael Gasper
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Gasper, R., Meyer, S., Gotthardt, K. et al. It takes two to tango: regulation of G proteins by dimerization. Nat Rev Mol Cell Biol 10, 423–429 (2009). https://doi.org/10.1038/nrm2689

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