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Rab11a and Rab8a are ubiquitous small GTPases shown as required for rhodopsin transport in  Xenopus laevis  and zebrafish photoreceptors by dominant negative (dn) disruption of function. Here, we generated retina-specific  Rab11a  ( ret  Rab11a ) and  Rab8a  ( ret  Rab8a ) single and double knockout mice to explore the consequences in mouse photoreceptors. Rhodopsin and other outer segment (OS) membrane proteins targeted correctly to OS and electroretinogram (ERG) responses in all three mutant mouse lines were indistinguishable from wild-type (WT). Further, AAV (adeno-associated virus)-mediated expression of dnRab11b in  ret  Rab11a  -/-  retina, or expression of dnRab8b in  ret  Rab8a  -/-  retina did not cause OS protein mislocalization. Finally, a  ret  Rab8a  -/-  retina injected at one month of age with AAVs expressing dnRab11a, dnRab11b, dnRab8b, and dnRab10 (four dn viruses on  Rab8a  -/-  background) and harvested three months later exhibited normal OS protein localization. In contrast to results obtained with dnRab GTPases in  Xenopus  and zebrafish, mouse Rab11a and Rab8a are dispensable for proper rhodopsin and outer segment membrane protein targeting. Absence of phenotype after expression of four dn Rab GTPases in a  Rab8a  -/-  retina suggests that Rab8b and Rab11b paralogs maybe dispensable as well. Our data thus demonstrate significant interspecies variation in photoreceptor membrane protein and rhodopsin trafficking.

Small GTPases Rab8a and Rab11a Are Dispensable for Rhodopsin Transport in Mouse Photoreceptors