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Transgenic Analysis of Rds/Peripherin N ‐Glycosylation
Author(s) -
Kedzierski Wojciech,
Bok Dean,
Travis Gabriel H.
Publication year - 1999
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1046/j.1471-4159.1999.0720430.x
Subject(s) - peripherin , glycosylation , transgene , biology , glycoprotein , microbiology and biotechnology , glycan , biochemistry , gene
: Rds/peripherin is an integral membrane glycoprotein thatis present in the rims of photoreceptor outer segment disks. In mammals, it isthought to stabilize the disk rim through heterophilic interactions with therelated nonglycosylated protein rom1. Glycosylation of rds/peripherin atasparagine 229 is widely conserved in vertebrates. In this study, weinvestigated the role of rds/peripherin N ‐glycosylation. We generatedtransgenic mice that expressed only S231A‐substituted rds/peripherin in theirretinas. This protein was not glycosylated but formed covalent dimers withitself and with glycosylated rds/peripherin. Nonglycosylated rds/peripherinalso interacted noncovalently with rom1 homodimers to form a heterooligomericcomplex. The glycosylated rds/peripherin ·· rom1 complex boundto concanavalin A‐Sepharose, suggesting that the glycan is not directlyinvolved in the interaction between these proteins. In double transgenic miceexpressing normal and S231A‐substituted rds/peripherin, the mRNA‐to‐proteinratios were similar for both transgenes, indicating no effect of N ‐glycosylation on rds/peripherin stability. Finally, expression ofnonglycosylated rds/peripherin in transgenic mice rescued the phenotype ofouter segment nondevelopment in retinal degeneration slow (rds‐/‐) null mutants. These observations indicate that N ‐glycosylation of rds/peripherin is not required for its normal processing, stability, or in vivo function.