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The delta subunit of rod specific cyclic GMP phosphodiesterase, PDE δ, interacts with the Arf‐like protein Arl3 in a GTP specific manner
Author(s) -
Linari Marco,
Hanzal-Bayer Michael,
Becker Jörg
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)01117-5
Subject(s) - gtp' , nucleotide , phosphodiesterase , guanine , chemistry , guanine nucleotide exchange factor , immunoprecipitation , effector , protein subunit , gtp binding protein regulators , g protein , biochemistry , gtpase , biology , signal transduction , enzyme , gene
Recently, we have shown that the δ subunit of the cGMP phosphodiesterase (PDE δ) 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 δ. The interaction was verified by fluorescence spectroscopy and co‐immunoprecipitation. Arl3 features an unusually low affinity for guanine nucleotides, with a K D of 24 nM for GDP and 48 μM for GTP. Fluorescence spectroscopy shows that PDE δ binds and specifically stabilizes the GTP‐bound form of Arl3 by strongly decreasing the dissociation rate of GTP. Thus, PDE δ is an effector of Arl3 and could provide a novel nucleotide exchange mechanism by which PDE δ stabilizes Arl3 in its active GTP‐bound form.