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Published December 2016 | Accepted Version
Journal Article Open

ATPase and GTPase Tangos Drive Intracellular Protein Transport


The GTPase superfamily of proteins provides molecular switches to regulate numerous cellular processes. The 'GTPase switch' paradigm, in which external regulatory factors control the switch of a GTPase between 'on' and 'off' states, has been used to interpret the regulatory mechanism of many GTPases. However, recent work unveiled a class of nucleotide hydrolases that do not adhere to this classical paradigm. Instead, they use nucleotide-dependent dimerization cycles to regulate key cellular processes. In this review article, recent studies of dimeric GTPases and ATPases involved in intracellular protein targeting are summarized. It is suggested that these proteins can use the conformational plasticity at their dimer interface to generate multiple points of regulation, thereby providing the driving force and spatiotemporal coordination of complex cellular pathways.

Additional Information

© 2016 Elsevier. Available online 19 September 2016. The author thanks members of her laboratory for helpful comments on the manuscript. This work was supported by NIH grants GM078024 and GM107368 and by the Gordon and Betty Moore Foundation through Grant GBMF2939 to S.S.

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