Disruption of RPGR protein interaction network is the common feature of RPGR missense variations that cause XLRP.

ABSTRACT: Retinitis pigmentosa (RP) is an inherited retinal degenerative disease with severe vision impairment leading to blindness. About 10-15% of RP cases are caused by mutations in the RPGR gene, with RPGR mutations accounting for 70% of X-linked RP cases. The mechanism by which RPGR mutations cause photoreceptor cell dysfunction is not well understood. In this study, we show that the two isoforms of RPGR (RPGR^1-19 and RPGR^ORF15) interact with endogenous PDE6D, INPP5E, and RPGRIP1L. The RPGR^1-19 isoform contains two PDE6D binding sites with the C-terminal prenylation site being the predominant PDE6D binding site. The C terminus of RPGR^1-19 that contains the prenylation site regulates its interaction with PDE6D, INPP5E, and RPGRIP1L. Only the RPG

SUBMITTER: Zhang Q 

PROVIDER: S-EPMC6347721 | biostudies-literature | 2019 Jan

REPOSITORIES: biostudies-literature