July 2019
Volume 60, Issue 9
Open Access
ARVO Annual Meeting Abstract  |   July 2019
The Congenital Cataract Mutation E151K in Vimentin Creates A SUMOylation Site Allowing in Vivo Sumoylation, Preventing Its Polymerization, and Leading to Cataractogenesis
Author Affiliations & Notes
  • xiaodong gong
    Zhongshan Ophthalmic Center, Sun Yat-sen university, Guangzhou, China
  • David W Li
    Zhongshan Ophthalmic Center, Sun Yat-sen university, Guangzhou, China
  • Footnotes
    Commercial Relationships   xiaodong gong, None; David Li, None
  • Footnotes
    Support  (Supported by the grant, 81570824, from the National Natural Science Foundation of China, and the Fundamental Funds of the State Key Laboratory of Ophthalmology of Zhongshan Ophthalmic Center, and the Graduate Scholarship from Sun Yat-sen University).
Investigative Ophthalmology & Visual Science July 2019, Vol.60, 1382. doi:
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      xiaodong gong, David W Li; The Congenital Cataract Mutation E151K in Vimentin Creates A SUMOylation Site Allowing in Vivo Sumoylation, Preventing Its Polymerization, and Leading to Cataractogenesis. Invest. Ophthalmol. Vis. Sci. 2019;60(9):1382.

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

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Abstract

Purpose : The E151K mutation in vimentin causes congenital cataractogenesis. However, the molecular mechanism remains largely unknown. Here we present evidence to reveal the plausible mechanism.

Methods : RT-PCR was used to clone the wild type vimentin cDNA. In vitro mutagenesis was used to create the E151K mutant cDNAs. Expression constructs of both wild type and mutant cDNAs were introduced into lens epithelial cells, the sumoylation patterns were determined by Western blot analysis. Chemical crosslink was used to help the determination of vimentin polymers. Cell morphology and microfilament polymerization were observed with fluorescence imaging. Vimentin polymerization under various conditions were detected by Western blot analysis.

Results : Wild type and mutant vimentin display differential SUMOylation patterns. Sumoylation in the mutant protein interferes with vimentin polymerization, and thus inhibiting its normal functions.

Conclusions : The molecular basis for E151K mutation causing cataractogenesis is due to the generation of the novel sumoylation site in the mutant molecule. (Supported by the grant, 81570824, from the National Natural Science Foundation of China, and the Fundamental Funds of the State Key Laboratory of Ophthalmology of Zhongshan Ophthalmic Center, and the Graduate Scholarship from Sun Yat-sen University).

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

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