The delta subunit of rod specific cyclic GMP phosphodiesterase, PDE delta, interacts with the Arf-like protein Arl3 in a GTP specific manner.
Recently, we have shown that the delta subunit of the cGMP phosphodiesterase (PDE delta) interacts with the retinitis pigmentosa guanine regulator (RPGR). Here, using the two-hybrid system, we identify a member of the Arf-like protein family of Ras-related GTP-binding proteins, Arl3, that interacts with PDE delta. The interaction was verified ... by fluorescence spectroscopy and co-immunoprecipitation. Arl3 features an unusually low affinity for guanine nucleotides, with a KD of 24 nM for GDP and 48 microM for GTP. Fluorescence spectroscopy shows that PDE delta binds and specifically stabilizes the GTP-bound form of Arl3 by strongly decreasing the dissociation rate of GTP. Thus, PDE delta is an effector of Arl3 and could provide a novel nucleotide exchange mechanism by which PDE delta stabilizes Arl3 in its active GTP-bound form.
Mesh Terms:
3',5'-Cyclic-GMP Phosphodiesterases, ADP-Ribosylation Factors, Animals, Cell Line, Cyclic Nucleotide Phosphodiesterases, Type 6, Eye Proteins, Guanosine Triphosphate, Humans, Kinetics, Mice, Mutagenesis, Plasmids, Protein Conformation, Spectrometry, Fluorescence, Time Factors, Transfection, Two-Hybrid System Techniques
3',5'-Cyclic-GMP Phosphodiesterases, ADP-Ribosylation Factors, Animals, Cell Line, Cyclic Nucleotide Phosphodiesterases, Type 6, Eye Proteins, Guanosine Triphosphate, Humans, Kinetics, Mice, Mutagenesis, Plasmids, Protein Conformation, Spectrometry, Fluorescence, Time Factors, Transfection, Two-Hybrid System Techniques
FEBS Lett.
Date: Sep. 10, 1999
PubMed ID: 10518933
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