arginyl-glycyl-serine and tetrafluoroaluminate

arginyl-glycyl-serine has been researched along with tetrafluoroaluminate* in 1 studies

Other Studies

1 other study(ies) available for arginyl-glycyl-serine and tetrafluoroaluminate

ArticleYear
RGS12 and RGS14 GoLoco motifs are G alpha(i) interaction sites with guanine nucleotide dissociation inhibitor Activity.
    The Journal of biological chemistry, 2001, Aug-03, Volume: 276, Issue:31

    The regulators of G-protein signaling (RGS) proteins accelerate the intrinsic guanosine triphosphatase activity of heterotrimeric G-protein alpha subunits and are thus recognized as key modulators of G-protein-coupled receptor signaling. RGS12 and RGS14 contain not only the hallmark RGS box responsible for GTPase-accelerating activity but also a single G alpha(i/o)-Loco (GoLoco) motif predicted to represent a second G alpha interaction site. Here, we describe functional characterization of the GoLoco motif regions of RGS12 and RGS14. Both regions interact exclusively with G alpha(i1), G alpha(i2), and G alpha(i3) in their GDP-bound forms. In GTP gamma S binding assays, both regions exhibit guanine nucleotide dissociation inhibitor (GDI) activity, inhibiting the rate of exchange of GDP for GTP by G alpha(i1). Both regions also stabilize G alpha(i1) in its GDP-bound form, inhibiting the increase in intrinsic tryptophan fluorescence stimulated by AlF(4)(-). Our results indicate that both RGS12 and RGS14 harbor two distinctly different G alpha interaction sites: a previously recognized N-terminal RGS box possessing G alpha(i/o) GAP activity and a C-terminal GoLoco region exhibiting G alpha(i) GDI activity. The presence of two, independent G alpha interaction sites suggests that RGS12 and RGS14 participate in a complex coordination of G-protein signaling beyond simple G alpha GAP activity.

    Topics: Aluminum Compounds; Amino Acid Sequence; Amino Acid Substitution; Animals; Binding Sites; Biosensing Techniques; Cloning, Molecular; Escherichia coli; Fluorides; Guanosine 5'-O-(3-Thiotriphosphate); Guanosine Diphosphate; Heterotrimeric GTP-Binding Proteins; Kinetics; Models, Biological; Molecular Sequence Data; Mutagenesis, Site-Directed; Oligopeptides; Open Reading Frames; Rats; Recombinant Proteins; RGS Proteins; Signal Transduction; Surface Plasmon Resonance

2001