Assay and functional properties of PrBP(PDEδ), a prenyl-binding protein interacting with multiple partners.

Abstract

Abstract

A 17-kDa prenyl-binding protein, PrBP(PDEδ), is highly conserved among various species from human to Caenorhabditis elegans. First identified as a putative regulatory δ subunit of the cyclic nucleotide phosphodiesterase (PDE6) purified from mammalian photoreceptor cells, PrBP(PDEδ) has been hypothesized to reduce activation of PDE6 by the heterotrimeric G-protein, transducin, thereby desensitizing the photoresponse. However, recent work shows that PrBP(PDEδ) interacts with numerous prenylated proteins at their farnesylated or geranylgeranylated C-termini, as well as with nonprenylated proteins. These polypeptides include small GTPases such as Rab13, Ras, Rap, and Rho6, as well as components involved in phototransduction (e.g., rod and cone PDE6, rod and cone opsin kinases). Expression of PrBP(PDEδ) in tissues and organisms not expressing PDE6, the demonstration of multiple interacting partners with PrBP(PDEδ), and its low abundance in rod outer segments all argue against it being a regulatory PDE6 subunit. This raises intriguing questions as to its physiological functions. In this chapter, we review the current status of PrBP(PDEδ) and describe some of the assays used to determine these interactions in detail. In mammalian photoreceptors, the results are consistent with a role of PrBP(PDEδ) in the transport of prenylated proteins from their site of synthesis in the inner segment to the outer segment where phototransduction occurs.

Department

Molecular, Cellular and Biomedical Sciences

Publication Date

2005

Journal Title

Methods in Enzymology

Publisher

Elsevier

Digital Object Identifier (DOI)

10.1016/S0076-6879(05)03005-3

Document Type

Article

Rights

Copyright 2005, Elsevier Inc. All rights reserved.

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