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Biochem Soc Trans. 2018 Dec 17;46(6):1713-1720. doi: 10.1042/BST20180481. Epub 2018 Dec 4.

PseudoGTPase domains in p190RhoGAP proteins: a mini-review.

Author information

1
Department of Pharmacology, Yale University School of Medicine, 333 Cedar Street, New Haven, CT 06520, U.S.A.
2
Department of Pharmacology, Yale University School of Medicine, 333 Cedar Street, New Haven, CT 06520, U.S.A. titus.boggon@yale.edu.
3
Department of Molecular Biophysics and Biochemistry, Yale University School of Medicine, 333 Cedar Street, New Haven, CT 06520, U.S.A.
4
Yale Cancer Center, Yale University School of Medicine, 333 Cedar Street, New Haven, CT 06520, U.S.A.

Abstract

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.

KEYWORDS:

p190RhoGAP; pseudoGTPase; pseudoenzyme; pseudokinase; rho signaling; small GTPase

PMID:
30514771
DOI:
10.1042/BST20180481
[Indexed for MEDLINE]

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