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

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Publication Type Journal Article
School or College College of Pharmacy; College of Science; College of Engineering; School of Medicine
Department Chemistry; Ophthalmology; Biochemistry; Medicinal Chemistry; Bioengineering
Creator Baehr, Wolfgang; Prestwich, Glenn D.
Other Author Zhang, Houbin; Liu, Xiao-hui; Zhang, Kai; Chen, Ching-Kang; Frederick, Jeanne M.
Title Photoreceptor cGMP phosphodiesterase delta subunit (PDEdelta) functions as a prenyl-binding protein
Date 2004
Description 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 is present in rods and cones. We find by yeast two-hybrid screening with a PDEdelta bait that it can interact with farnesylated rhodopsin kinase (GRK1) and that prenylation is essential for this interaction. In vitro binding assays indicate that both recombinant farnesylated GRK1 and geranylgeranylated GRK7 co-precipitate with a glutathione S-transferase-PDEdelta fusion protein. Using fluorescence resonance energy transfer techniques exploiting the intrinsic tryptophan fluorescence of PDEdelta and dansylated prenyl cysteines as fluorescent ligands, we show that PDEdelta specifically binds geranylgeranyl and farnesyl moieties with a Kd of 19.06 and 0.70 microm, respectively. Our experiments establish that PDEdelta functions as a prenyl-binding protein interacting with multiple prenylated proteins.
Type Text
Publisher American Society for Biochemistry and Molecular Biology (ASBMB)
Volume 279
Issue 1
First Page 407
Last Page 413
Subject Fluorescence Resonance Energy Transfer; GTP Phosphohydrolases; Immunohistochemistry
Subject MESH Cysteine; Photoreceptors, Vertebrate; Rods (Retina)
Language eng
Bibliographic Citation Zhang H, Liu XH, Zhang K, Chen CK, Frederick JM, Prestwich GD, Baehr W. (2004). Photoreceptor cGMP phosphodiesterase delta subunit (PDEdelta) functions as a prenyl-binding protein. J Biol Chem, 279(1), 407-13
Rights Management (c)American Society for Biochemistry and Molecular Biology (ASBMB)
Format Medium application/pdf
Identifier ir-main,1734
ARK ark:/87278/s6rr2gqw
Setname ir_uspace
Date Created 2012-06-13
Date Modified 2012-06-13
ID 705831
Reference URL https://collections.lib.utah.edu/ark:/87278/s6rr2gqw
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