Retinal S-antigen (Sag or arrestin) has a high affinity for phosphorylated rhodopsin, but a low affinity for unphosphorylated rhodopsin. Arrestin binds to phosphorylated rhodopsin and blocks interaction with the G protein transducin, halting the phototransduction cascade.Mice that are homozygous for the targeted mutation develop disorganized photoreceptors and retinal degeneration when raised in cyclic light. Retinal degeneration is characterized by a progressive decrease in photoreceptor outer segment (OS) length and by progressive thinness of the outer nuclear layer (ONL). The 3A-50 transgene is altered to bind unphosphorylated rhodopsin and expresses mutant arrestin at 50% of wild type. When Sag -/- mice are combined with the low-expressing (3A-50) mutant arrestin (Sag) transgenics, the transgene rescues a portion of the KO phenotype preventing photoreceptor loss, but does not return OS length completely to wild-type levels. 

This mutant mouse strain may be useful in studies of retinal degeneration, light-dark adaptation and G protein-coupled receptor signaling.

Sag -/- (retinal S-antigen) mice develop disorganized photoreceptors and retinal degeneration when raised in cyclic light, when combined with the high-expressing (3A-50) mutant arrestin (Sag) transgenics, the transgene rescues a portion of the KO phenotype preventing photoreceptor loss, but does not return outer segment length completely to wild-type levels. 

This mutant mouse strain may be useful in studies of retinal degeneration, light-dark adaptation and G protein-coupled receptor signaling.

This strain is hosted by NIH's MMRRC, which partners with JAX for the distribution of this and other strains. For additional information and to purchase, please visit the MMRRC site.