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J. Biol. Chem., Vol. 279, Issue 40, 42202-42210, October 1, 2004

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Proteolytic Shedding of the Extracellular Domain of Photoreceptor Cadherin

IMPLICATIONS FOR OUTER SEGMENT ASSEMBLY^*

Amir Rattner, Jichao Chen, and Jeremy Nathans¶||**

From the Departments of Molecular Biology and Genetics, ^¶Neuroscience, and ^||Ophthalmology and the ^**Howard Hughes Medical Institute, The Johns Hopkins University School of Medicine, Baltimore, Maryland 21205

Photoreceptor cadherin (prCAD) is a distinctive cadherin family member that is concentrated at the base of rod and cone outer segments and is required for their structural integrity. During retinal development, prCAD localizes to the site of the future outer segment before rhodopsin or other phototransduction proteins. In vivo, prCAD undergoes a single proteolytic cleavage that releases the ectodomain as a soluble fragment. The C-terminal fragment containing the transmembrane and cytosolic domains remains associated with the outer segment. In rds(-/-) retinas, in which outer segment assembly is severely disrupted because of the absence of retinal degeneration slow (RDS)/peripherin, an essential outer segment structural protein, the level of prCAD is increased, whereas the levels of other outer segment proteins are decreased relative to wild type retinas. Additionally, the ratio of intact:cleaved prCAD polypeptides is increased in rds(-/-) retinas. These data imply that prCAD ectodomain cleavage is an integral part of the outer segment assembly process, and they further suggest that outer segment assembly might be driven, at least in part, by the near irreversibility of proteolysis.

Received for publication, July 14, 2004 , and in revised form, July 27, 2004.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBank^TM/EBI Data Bank with accession number(s) AY683207 and AY684930.

^* This work was supported by the NEI, National Institutes of Health and by the Howard Hughes Medical Institute. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

To whom correspondence should be addressed: 805 PCTB, 725 N. Wolfe St., The Johns Hopkins University School of Medicine, Baltimore, MD 21205. Tel.: 410-955-4679; Fax: 410-614-0827; E-mail: arattner{at}jhmi.edu.

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