Cookies on this website
We use cookies to ensure that we give you the best experience on our website. If you click 'Continue' we'll assume that you are happy to receive all cookies and you won't see this message again. Click 'Find out more' for information on how to change your cookie settings.

Centaurins are a family of proteins that contain GTPase-activating protein domains, with the gamma family members containing in addition a GTPase-like domain. Centaurins reside mainly in the nucleus and are known to activate phosphoinositide 3-kinase, a key regulator of cell proliferation, motility and vesicular trafficking. In the present study, using X-ray structural analysis, enzymatic assays and nucleotide-binding studies, we show that, for CENTG1 (centaurin gamma-1) the GTPase-like domain has broader trinucleotide specificity. Alterations within the G4 motif of CENTG1 from the highly conserved NKXD found in typical GTPases to TQDR result in the loss of specificity, a lower affinity for the nucleotides and higher turnover rates. These results indicate that the centaurins could be more accurately classified as NTPases and point to alternative mechanisms of cell signalling control.

Original publication

DOI

10.1042/BJ20060555

Type

Journal article

Journal

Biochem J

Publication Date

01/02/2007

Volume

401

Pages

679 - 688

Keywords

Amino Acid Sequence, Binding Sites, Cloning, Molecular, Escherichia coli, GTP-Binding Proteins, GTPase-Activating Proteins, Hydrolysis, Models, Molecular, Molecular Structure, Nucleoside-Triphosphatase, Nucleotides, Protein Structure, Tertiary, Signal Transduction, Substrate Specificity, ras Proteins