Pseudoenzymes generally lack detectable catalytic activity despite adopting the overall protein fold of their catalytically competent counterparts, indeed ‘pseudo’ family members seem to be incorporated in all enzyme classes. The small GTPase enzymes are important signaling proteins, and recent studies have identified many new family members with noncanonical residues within the catalytic cleft, termed pseudoGTPases. To illustrate recent discoveries in the field, we use the p190RhoGAP proteins as an example. p190RhoGAP proteins (ARHGAP5 and ARHGAP35) are the most abundant GTPase activating proteins for the Rho family of small GTPases. These are key regulators of Rho signaling in processes such as cell migration, adhesion and cytokinesis. Structural biology has complemented and guided biochemical analyses for these proteins and has allowed discovery of two cryptic pseudoGTPase domains, and the re-classification of a third, previously identified, GTPase-fold domain as a pseudoGTPase. The three domains within p190RhoGAP proteins illustrate the diversity of this rapidly expanding pseudoGTPase group.
Review Article| December 04 2018
PseudoGTPase domains in p190RhoGAP proteins: a mini-review
Amy L. Stiegler;
Titus J. Boggon
1Department of Pharmacology, Yale University School of Medicine, 333 Cedar Street, New Haven, CT 06520, U.S.A.
2Department of Molecular Biophysics and Biochemistry, Yale University School of Medicine, 333 Cedar Street, New Haven, CT 06520, U.S.A.
3Yale Cancer Center, Yale University School of Medicine, 333 Cedar Street, New Haven, CT 06520, U.S.A.
Correspondence: Titus J. Boggon (firstname.lastname@example.org)
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Amy L. Stiegler, Titus J. Boggon; PseudoGTPase domains in p190RhoGAP proteins: a mini-review. Biochem Soc Trans 17 December 2018; 46 (6): 1713–1720. doi: https://doi.org/10.1042/BST20180481
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