Photoreceptor cGMP phosphodiesterase delta subunit (PDEdelta) functions as a prenyl-binding protein.

@article{Zhang2004PhotoreceptorCP,
  title={Photoreceptor cGMP phosphodiesterase delta subunit (PDEdelta) functions as a prenyl-binding protein.},
  author={Houbin Zhang and Xiaoming Liu and Kai Zhang and Ching-Kang Jason Chen and Jeanne Marie Frederick and Glenn D. Prestwich and Wolfgang Baehr},
  journal={The Journal of biological chemistry},
  year={2004},
  volume={279 1},
  pages={
          407-13
        }
}
Bovine PDEdelta was originally copurified with rod cGMP phosphodiesterase (PDE) and shown to interact with prenylated, carboxymethylated C-terminal Cys residues. Other studies showed that PDEdelta can interact with several small GTPases including Rab13, Ras, Rap, and Rho6, all of which are prenylated, as well as the N-terminal portion of retinitis pigmentosa GTPase regulator and Arl2/Arl3, which are not prenylated. We show by immunocytochemistry with a PDEdelta-specific antibody that PDEdelta… CONTINUE READING

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