July 2019
Volume 60, Issue 9
Open Access
ARVO Annual Meeting Abstract  |   July 2019
Loss of CEP290 causes accumulation of inner segment plasma membrane proteins in the outer segment
Author Affiliations & Notes
  • Seongjin Seo
    Ophthalmology and Visual Sciences, University of Iowa, Iowa City, Iowa, United States
    Institute for Vision Research, Iowa City, Iowa, United States
  • Poppy Datta
    Ophthalmology and Visual Sciences, University of Iowa, Iowa City, Iowa, United States
    Institute for Vision Research, Iowa City, Iowa, United States
  • Brandon Hendrickson
    Ophthalmology and Visual Sciences, University of Iowa, Iowa City, Iowa, United States
    Institute for Vision Research, Iowa City, Iowa, United States
  • Footnotes
    Commercial Relationships   Seongjin Seo, None; Poppy Datta, None; Brandon Hendrickson, None
  • Footnotes
    Support  NIH Grants R01EY022616 and R21EY027431
Investigative Ophthalmology & Visual Science July 2019, Vol.60, 3980. doi:
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      Seongjin Seo, Poppy Datta, Brandon Hendrickson; Loss of CEP290 causes accumulation of inner segment plasma membrane proteins in the outer segment. Invest. Ophthalmol. Vis. Sci. 2019;60(9):3980.

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

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Abstract

Purpose : Mutations in CEP290 cause Leber congenital amaurosis (LCA). The current study is to determine molecular functions of CEP290 in photoreceptors and identify disease mechanisms of CEP290-associated LCA.

Methods : Localization of various inner segment- and outer segment-specific proteins was evaluated by immunohistochemistry in Cep290 conditional and rd16 mutant mouse retinas as well as by immunoblot analyses of isolated outer segments. iCre75 transgenic mice were used to inactivate Cep290 expression in rod photoreceptors.

Results : Localization of most outer segment-specific proteins was not altered in CEP290 deficient photoreceptors. One notable exception was rhodopsin, which showed significant mislocalization in the inner segment at all stages of degeneration. In contrast, mislocalization of inner segment proteins in the outer segment was more pronounced. In particular, depletion of CEP290 caused rapid accumulation of inner segment proteins STX3 and STXBP1, which are known to mislocalize in Bardet-Biedl syndrome (BBS) mutant retinas, in the outer segment. Among STX3 interacting proteins, SNAP25, which normally localizes to the inner segment plasma membrane, also showed significant mislocalization to the outer segment. Other inner segment plasma membrane proteins tested, including IMPG2 and Na+/K+-ATPase1, showed various degrees of mislocalization to the outer segment. In contrast, localization of endomembrane proteins including VAMP2, a v-SNARE protein localizing to secretory vesicles, was not affected.

Conclusions : Our data indicate that CEP290 is necessary to maintain compartment-specific protein localization in photoreceptors, particularly to prevent mislocalization of inner segment plasma membrane proteins to the outer segment. CEP290 is also needed for outer segment-specific localization of rhodopsin. These data demonstrate that photoreceptor degeneration in CEP290-LCA is associated with disruption of compartmentalized protein localization.

This abstract was presented at the 2019 ARVO Annual Meeting, held in Vancouver, Canada, April 28 - May 2, 2019.

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