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J. Biol. Chem., Vol. 275, Issue 32, 24752-24759, August 11, 2000

This Article Full Text Full Text (PDF) All Versions of this Article: 275/32/24752    most recent M002668200v1 Submit a Letter to Editor Alert me when this article is cited Alert me when eLetters are posted Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Request Permissions Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Webel, R. Articles by Colley, N. J. Search for Related Content PubMed PubMed Citation Articles by Webel, R. Articles by Colley, N. J. Social Bookmarking                      What's this?

Role of Asparagine-linked Oligosaccharides in Rhodopsin Maturation and Association with Its Molecular Chaperone, NinaA^*

Rebecca Webel, Indu Menon, Joseph E. O'Tousa^§, and Nansi Jo Colley^¶

From the  Department of Ophthalmology & Visual Science and the Department of Genetics, University of Wisconsin, Madison, Wisconsin 53706 and the ^§ Department of Biological Sciences, University of Notre Dame, Notre Dame, Indiana 46556

Many proteins require N-linked glycosylation for conformational maturation and interaction with their molecular chaperones. In Drosophila, rhodopsin (Rh1), the most abundant rhodopsin, is glycosylated in the endoplasmic reticulum (ER) and requires its molecular chaperone, NinaA, for exit from the ER and transport through the secretory pathway. Studies of vertebrate rhodopsins have generated several conflicting proposals regarding the role of glycosylation in rhodopsin maturation. We investigated the role of Rh1 glycosylation and Rh1/NinaA interactions under in vivo conditions by analyzing transgenic flies expressing Rh1 with isoleucine substitutions at each of the two consensus sites for N-linked glycosylation (N20I and N196I). We show that Asn²⁰ is the sole site for glycosylation. The Rh1^N20I protein is retained within the secretory pathway, causing an accumulation of ER cisternae and dilation of the Golgi complex. NinaA associates with nonglycosylated Rh1^N20I; therefore, retention of nonglycosylated rhodopsin within the ER is not due to the lack of Rh1^N20I/NinaA interaction. We further show that Rh1^N20I interferes with wild type Rh1 maturation and triggers a dominant form of retinal degeneration. We conclude that during maturation Rh1 is present in protein complexes containing NinaA and that Rh1 glycosylation is required for transport of the complexes through the secretory pathway. Failure of this transport process leads to retinal degeneration.

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