April 2014
Volume 55, Issue 13
Free
ARVO Annual Meeting Abstract  |   April 2014
Retinitis Pigmentosa 2 regulates transport of isoprenylated proteins to photoreceptor outer segments
Author Affiliations & Notes
  • Houbin Zhang
    Sichuan Academy of Medical Sciences &Sichuan Provincial People’s Hospital, Chengdu, China
    Ophthalmology, University of Utah, Salt Lake City, UT
  • Li Jiang
    Ophthalmology, University of Utah, Salt Lake City, UT
  • Christin Hanke
    Ophthalmology, University of Utah, Salt Lake City, UT
    Biochemistry and Biology, University of Potsdam, Potsdam-Golm, Germany
  • Wolfgang Baehr
    Ophthalmology, University of Utah, Salt Lake City, UT
  • Footnotes
    Commercial Relationships Houbin Zhang, None; Li Jiang, None; Christin Hanke, None; Wolfgang Baehr, None
  • Footnotes
    Support None
Investigative Ophthalmology & Visual Science April 2014, Vol.55, 420. doi:
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    • Get Citation

      Houbin Zhang, Li Jiang, Christin Hanke, Wolfgang Baehr; Retinitis Pigmentosa 2 regulates transport of isoprenylated proteins to photoreceptor outer segments. Invest. Ophthalmol. Vis. Sci. 2014;55(13):420.

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      © ARVO (1962-2015); The Authors (2016-present)

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Abstract

Purpose: X-linked retinitis pigmentosa (XLRP) is a devastating form of retinal degeneration, manifesting early in life with symptoms of night blindness, visual field defects, and decreased visual function. In-vitro, RP2 functions as a GAP for the small GTPase ARL3, a GDI displacement factor (GDF). Mutations in the Rp2 gene account for approximately one quarter of all XLRPs. The purpose of this study was to investigate the consequences of RP2 deletion and identify mechanisms causative of XLRP.

Methods: Intracellular localization of RP2 in photoreceptors was determined by neonatal electroporation of an RP2-EGFP expression vector. An Rp2 knockout mouse was generated using a EUCOMM ES cell line containing a gene trap in intron 1. The knockout mice were characterized by Western blot, immunocytochemistry, and electroretinography (ERG).

Results: RP2-eGFP was localized to the plasma membrane of inner segments, axons and synaptic termini in photoreceptors, but not in outer segments. The Rp2 gene knockout mice were viable and developed normally. Ablation of Rp2 gene expression led to slowly progressing degeneration of cone and rod photoreceptors as indicated by ERG recordings. Scotopic a-wave and photopic b wave amplitudes were reduced as early as one month of age in the knockout mice. The Rp2Y/- ERG amplitudes were further reduced at 6 months of age. Trafficking of transmembrane phototransduction proteins, including cone opsins, to Rp2Y/- photoreceptors outer segments was normal up to 14 months of age. While targeting of transducin α and βγ to the Rp2Y/- outer segments was not affected in the knockout, transport of rod and cone PDE6 as well as GRK1 to outer segments was impeded.

Conclusions: RP2 is distributed to plasma membrane of inner segments and synaptic termini in photoreceptors. RP2 is not essential for trafficking cone opsins and transducin to photoreceptor outer segments, but regulates transport of isoprenylated proteins to photoreceptor outer segments. Our results suggest that RP2/ARL3 may allosterically release prenylated proteins from their soluble complex with PDE6D and unload them to donor membranes (e.g., TGN vesicles). ). In the Rp2 knockout, this process is impeded.

Keywords: 702 retinitis • 695 retinal degenerations: cell biology • 648 photoreceptors  
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