GTPases

GTPases are a large family of hydrolase enzymes that bind to the nucleotide guanosine triphosphate (GTP) and hydrolyze it to guanosine diphosphate (GDP).   GTPases act as molecular switches that alternate between two distinct conformations, active or inactive, depending on whether they are bound to GTP (active) or GDP (inactive).  There are six main families of GTPases; heterotrimeric G protein GTPases, small monomeric GTPases, protein-synthesizing GTPases, signal-recognition particle GTPases, dynamin GTPases and tubulin GTPases.  The ability of GTPases  to function as molecular switches or timers makes them important in many cellular processes including signal transduction, protein synthesis and translocation, control of cell growth and differentiation, and vesicular transport regulation.  Dysfunction of GTPases is associated with multiple human diseases, including neurodegeneration, cardiovascular disease, cancer, and infections.

Further reading

Gilman (1987) G proteins: transducers of receptor-generated signals. Annu Rev Biochem. 56 615 PMID: 3113327

Maracci and Rodnina (2016) Review: Translational GTPases. Biopolymers 105(8) 463 PMID: 26971860

Flentje et al (2019) Small GTPases and Their Role in Vascular Disease. Int J Mol Sci. 20(4) 917 PMID: 30791562