Title |
The delta subunit of rod specific cyclic GMP phosphodiesterase, PDE δ, interacts with the Arf‐like protein Arl3 in a GTP specific manner
|
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Published in |
Febs Letters, September 1999
|
DOI | 10.1016/s0014-5793(99)01117-5 |
Pubmed ID | |
Authors |
Marco Linari, Michael Hanzal-Bayer, Jörg Becker |
Abstract |
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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Demographic breakdown
Readers by professional status | Count | As % |
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Student > Ph. D. Student | 6 | 16% |
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Other | 3 | 8% |
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Unknown | 4 | 11% |
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Medicine and Dentistry | 1 | 3% |
Other | 1 | 3% |
Unknown | 5 | 13% |