Arl3 and RP2 mediated assembly and traffic of membrane associated cilia proteins

The traffic of proteins to the outer segment of photoreceptors is a fundamentally important process, which when perturbed results in photoreceptor cell death. Recent reports have revealed a novel pathway for the traffic of lipid-modified proteins involving the small GTPase Arl3 and its effectors PDE delta and Unc119. The retinitis pigmentosa protein RP2 is a GTPase activating protein (GAP) for Arl3 and also appears to regulate the assembly and traffic of membrane associated protein complexes. We recently identified the G beta subunit of transducin (G beta 1) as a novel RP2 interacting protein. Our data support a role for RP2 in facilitating membrane association and traffic of G beta 1, potentially prior to the formation of the obligate G beta:G gamma heterodimer. Here, we review the recent evidence that suggests that RP2 co-operates with Arl3 and its effectors in protein complex assembly and membrane specification for lipid-modified proteins. This is exemplified by the co-ordination of cilia associated traffic for heterotrimeric G proteins and we propose a model for the role of Arl3 and RP2 in this process. (C) 2012 Elsevier Ltd. All rights reserved.