Phosphodiesterase 6D, cGMP-specific rod delta

Abstract

The Pde6d gene encodes a prenyl-binding protein (PrBPδ), first identified in bovine retinal extracts as a putative regulatory δ subunit of cyclic nucleotide phosphodiesterase (PDE6). It was hypothesized that PrBPδ reduced activation of PDE6 by desensitizing the photoresponse. However, PrBPδ is highly conserved among various species from human to Caenorhabditis elegans and has been shown to interact with numerous prenylated proteins at farnesylated or geranylgeranylated C-termini, as well as with non-prenylated proteins. In mammalian photoreceptor cells, PrBPδ has been shown to play a role in the transport of prenylated proteins from the inner segment (the site of protein synthesis) to their final destination in the outer segment where phototransduction occurs. In other cell types, PrBPδ interacts with a number of different monomeric GTPases and has been theorized to play a role in vesicular transport. Based on its crystal structure (an immunoglobulin-like fold that comprises a prenyl binding pocket), primary sequence comparisons, and structural homology modeling, the 17-kDa PrBPδ protein is highly conserved through evolution and represents the smallest member of a superfamily of prenyl-binding proteins that includes Unc119/RG4 and Rho GDP-dissociation inhibitor (RhoGDI).

Alternative names for this molecule: Pde6d; Phosphodiesterase 6D, cGMP-specific rod delta; Phosphodiesterase 6D, cGMP-specific, rod, delta; PrBP/delta; Prenyl binding protein/delta This molecule exists in 10 states and has 9 transitions between these states.

Department

Molecular, Cellular and Biomedical Sciences

Publication Date

1-18-2011

Journal Title

UCSD Nature Molecule Pages

Publisher

UCSD Signaling Gateway

Digital Object Identifier (DOI)

10.1038/mp.a001757.01

Document Type

Article

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