Retinitis pigmentosa-associated rhodopsin mutations in three membrane-located cysteine residues present three different biochemical phenotypes.
A large number of mutations in rhodopsin are associated with autosomal dominant retinitis pigmentosa (ADRP). We analyzed the biochemical phenotypes of the ADRP-associated cysteine mutants C167R, C222R, and C264del. C222R behaved as wild type in every aspect testable and is classified as a class I mutant. C167R produced intact protein but did not regenerate with 11-cis retinal and was not transported to the plasma membrane. We confirm its classification as a class IIa mutant. C264del represents a novel phenotype, which we propose to call class III. It produced a truncated protein of 27kDa that failed to regenerate with 11-cis retinal and was not targeted to the plasma membrane.
D000595:Amino Acid Sequence; D019943:Amino Acid Substitution; D000818:Animals; D002460:Cell Line; D003001:Cloning, Molecular; D003545:Cysteine; D003624:Darkness; D015870:Gene Expression; D006801:Humans; D008027:Light; D008969:Molecular Sequence Data; D010641:Phenotype; D011487:Protein Conformation; D017510:Protein Folding; D011994:Recombinant Proteins / Q000737:chemistry; D012174:Retinitis Pigmentosa / Q000145:classification / Q000235:genetics*; D012243:Rhodopsin / Q000235:genetics*; D013053:Spectrophotometry; D018411:Spodoptera; D014162:Transfection
D011994:Recombinant Proteins; D012243:Rhodopsin; D003545:Cysteine