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Human Molecular Genetics Advance Access published online on December 2, 2008
Human Molecular Genetics, doi:10.1093/hmg/ddn406
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© The Author 2008. Published by Oxford University Press. All rights reserved. For Permissions, please email: journals.permissions@oxfordjournals.org

Differential Requirements for Rds Intermolecular Disulfide-Linked Oligomerization in Rods Versus Cones

Dibyendu Chakraborty1, Xi-Qin Ding1, Shannon M. Conley1, Steven J. Fliesler2,§ and Muna I. Naash1,*

1 Department of Cell Biology, University of Oklahoma Health Sciences Center, Oklahoma City, OK 73104, U.S.A. 2 Departments of Ophthalmology and Pharmacological & Physiological Science, Saint Louis University School of Medicine, St. Louis, MO 63104, U.S.A

* To whom correspondence should be addressed: Muna I. Naash, Ph.D., Department of Cell Biology, University of Oklahoma Health Sciences Center, 940 Stanton L. Young Blvd., BMSB 781, Oklahoma City, OK- 73126-0901, U.S.A. Tel: 405- 271-8001 ex 47969; Fax : 405-271-3548; E-mail: muna-naash{at}ouhsc.edu.

Received October 6, 2008; Revised November 13, 2008; Accepted November 27, 2008

It is commonly assumed that the ultrastructural organization of the rim region of outer segment (OS) discs in rods and lamellae in cones requires functional Rds/Rom-1 complexes. Cysteine-150 (C150) in Rds has been implicated in intermolecular disulfide bonding essential for functional Rds complexes. Transgenic mice containing the Rds C150S mutation (C150S-Rds) failed to form higher-order Rds oligomers, although interactions between C150S-Rds and Rom-1 occurred in rods, but not in cones. C150S-Rds mice exhibited marked early-onset reductions in cone function and abnormal OS structure. In contrast, C150S-Rds expression in rods partly rescued the rds+/- phenotype. Although C150S-Rds was detected in the OSs in rods and cones, a substantial percentage of C150S-Rds and cone opsins were mislocalized to different cellular compartments in cones. The results of this study provide novel insights into the importance of C150 in Rds oligomerization and the differences in Rds requirements in rods vs. cones. The apparent OS structural differences between rods and cones may cause cones to be more susceptible to the elimination of higher-order Rds/Rom-1 oligomers (e.g., as mediated by mutation of the Rds C150 residue).

§ Current address: Department of Ophthalmology (Ross Eye Institute), University at Buffalo-S.U.N.Y, Buffalo, NY, and Research Service, Veterans Administration Western New York Healthcare System, Buffalo, NY 14215, U.S.A.


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