Abstract
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.
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Dates
Type | When |
---|---|
Created | 23 years, 1 month ago (July 25, 2002, 1:52 p.m.) |
Deposited | 1 year, 11 months ago (Sept. 16, 2023, 7:38 a.m.) |
Indexed | 2 months, 1 week ago (June 20, 2025, 12:06 p.m.) |
Issued | 25 years, 11 months ago (Sept. 3, 1999) |
Published | 25 years, 11 months ago (Sept. 3, 1999) |
Published Online | 25 years, 11 months ago (Sept. 3, 1999) |
Published Print | 25 years, 11 months ago (Sept. 10, 1999) |
@article{Linari_1999, title={The delta subunit of rod specific cyclic GMP phosphodiesterase, PDE δ, interacts with the Arf‐like protein Arl3 in a GTP specific manner}, volume={458}, ISSN={1873-3468}, url={http://dx.doi.org/10.1016/s0014-5793(99)01117-5}, DOI={10.1016/s0014-5793(99)01117-5}, number={1}, journal={FEBS Letters}, publisher={Wiley}, author={Linari, Marco and Hanzal-Bayer, Michael and Becker, Jörg}, year={1999}, month=sep, pages={55–59} }