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Title
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The delta subunit of rod specific cyclic GMP phosphodiesterase, PDE delta, interacts with the Arf-like protein Arl3 in a GTP specific manner.
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Authors
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M.Linari,
M.Hanzal-Bayer,
J.Becker.
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Ref.
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FEBS Lett, 1999,
458,
55-59.
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PubMed id
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Abstract
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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.
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