Retinitis pigmentosa-associated rhodopsin mutations in three membrane-located cysteine residues present three different biochemical phenotypes

Biochem Biophys Res Commun. 2002 Oct 4;297(4):847-53. doi: 10.1016/s0006-291x(02)02308-2.

Abstract

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.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Amino Acid Substitution
  • Animals
  • Cell Line
  • Cloning, Molecular
  • Cysteine*
  • Darkness
  • Gene Expression
  • Humans
  • Light
  • Molecular Sequence Data
  • Phenotype
  • Protein Conformation
  • Protein Folding
  • Recombinant Proteins / chemistry
  • Retinitis Pigmentosa / classification
  • Retinitis Pigmentosa / genetics*
  • Rhodopsin / genetics*
  • Spectrophotometry
  • Spodoptera
  • Transfection

Substances

  • Recombinant Proteins
  • Rhodopsin
  • Cysteine