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Journal of Neuroscience, Vol 14, 5818-5833, Copyright © 1994 by Society for Neuroscience

ARTICLE

A rhodopsin gene mutation responsible for autosomal dominant retinitis pigmentosa results in a protein that is defective in localization to the photoreceptor outer segment

CH Sung, C Makino, D Baylor and J Nathans
Department of Molecular Biology and Genetics, Johns Hopkins Medical School, Baltimore, Maryland 21205.

Over 45 mutations in the rhodopsin gene have been identified in patients with autosomal dominant retinitis pigmentosa, including a cluster near the extreme carboxy-terminus, a region of the protein for which no function has yet been assigned. To elucidate the biochemical defect(s) in this group of mutants, we have studied a naturally occurring stop codon mutation that removes the last five amino acids of rhodopsin (Q344ter). When produced in transfected tissue culture cells, the mutant protein is indistinguishable from the wild type in light- dependent activation of the photoreceptor G-protein (transducin), and in serving as a light-dependent substrate for rhodopskin kinase. Mice that express a Q344ter transgene in rod photoreceptors show nearly normal light responses as determined by suction electrode recordings of the membrane current from single rod outer segments; the main difference between transgenic and nontransgenic responses is a 15% longer time-to-peak in the response of transgenic rods. In the Q344ter transgenic retina, direct immunofluorescent staining with antibodies specific for either wild-type or Q344ter rhodopsin shows abnormal accumulation of the Q344ter, but not the endogenous rhodopsin, in the plasma membrane of the photoreceptor cell body. These data indicate that rhodopsin's carboxy-terminus is required for efficient transportation to or retention in the outer segment.


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J Chen, C. Makino, N. Peachey, D. Baylor, and M. Simon
Mechanisms of rhodopsin inactivation in vivo as revealed by a COOH-terminal truncation mutant
Science, January 20, 1995; 267(5196): 374 - 377.
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Rhodopsin plays an essential structural role in Drosophila photoreceptor development
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[Abstract] [PDF]

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T. Mirzadegan, F. Diehl, B. Ebi, S. Bhakta, I. Polsky, D. McCarley, M. Mulkins, G. S. Weatherhead, J.-M. Lapierre, J. Dankwardt, et al.
Identification of the Binding Site for a Novel Class of CCR2b Chemokine Receptor Antagonists. BINDING TO A COMMON CHEMOKINE RECEPTOR MOTIF WITHIN THE HELICAL BUNDLE
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R. Webel, I. Menon, J. E. O'Tousa, and N. J. Colley
Role of Asparagine-linked Oligosaccharides in Rhodopsin Maturation and Association with Its Molecular Chaperone, NinaA
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O. L. Moritz, B. M. Tam, D. S. Papermaster, and T. Nakayama
A Functional Rhodopsin-Green Fluorescent Protein Fusion Protein Localizes Correctly in Transgenic Xenopus laevis Retinal Rods and Is Expressed in a Time-dependent Pattern
J. Biol. Chem., July 20, 2001; 276(30): 28242 - 28251.
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S. Venkatesan, A. Petrovic, D. I. Van Ryk, M. Locati, D. Weissman, and P. M. Murphy
Reduced Cell Surface Expression of CCR5 in CCR5Delta 32 Heterozygotes Is Mediated by Gene Dosage, Rather Than by Receptor Sequestration
J. Biol. Chem., January 11, 2002; 277(3): 2287 - 2301.
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P. D. Alfinito and E. Townes-Anderson
Activation of mislocalized opsin kills rod cells: A novel mechanism for rod cell death in retinal disease
PNAS, April 16, 2002; 99(8): 5655 - 5660.
[Abstract] [Full Text] [PDF]

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P. D. Calvert, N. V. Krasnoperova, A. L. Lyubarsky, T. Isayama, M. Nicolo, B. Kosaras, G. Wong, K. S. Gannon, R. F. Margolskee, R. L. Sidman, et al.
Phototransduction in transgenic mice after targeted deletion of the rod transducin alpha -subunit
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