September 2016
Volume 57, Issue 12
Open Access
ARVO Annual Meeting Abstract  |   September 2016
SUMOylation Regulates Vimentin Functions in Lens
Author Affiliations & Notes
  • Ling Wang
    Zhongshan Ophthalmic Center, Sun Yat-sen University, Guangzhou, China
    Truhlsen Eye Institute, University of Nebraska Medical Center, Omaha, Nebraska, United States
  • Zhaoxia Huang
    Truhlsen Eye Institute, University of Nebraska Medical Center, Omaha, Nebraska, United States
    Zhongshan Ophthalmic Center, Sun Yat-sen University, Guangzhou, China
  • Xiaohui Hu
    Truhlsen Eye Institute, University of Nebraska Medical Center, Omaha, Nebraska, United States
    Zhongshan Ophthalmic Center, Sun Yat-sen University, Guangzhou, China
  • Yizhi Liu
    Zhongshan Ophthalmic Center, Sun Yat-sen University, Guangzhou, China
  • Quan Dong Nguyen
    Truhlsen Eye Institute, University of Nebraska Medical Center, Omaha, Nebraska, United States
  • David W Li
    Truhlsen Eye Institute, University of Nebraska Medical Center, Omaha, Nebraska, United States
    Zhongshan Ophthalmic Center, Sun Yat-sen University, Guangzhou, China
  • Footnotes
    Commercial Relationships   Ling Wang, None; Zhaoxia Huang, None; Xiaohui Hu, None; Yizhi Liu, None; Quan Dong Nguyen, None; David Li, None
  • Footnotes
    Support  Research Prevent Blindness, NSFC, Zhongshan Ophthalmic Center, Chinese Scholarship Council
Investigative Ophthalmology & Visual Science September 2016, Vol.57, No Pagination Specified. doi:
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    • Get Citation

      Ling Wang, Zhaoxia Huang, Xiaohui Hu, Yizhi Liu, Quan Dong Nguyen, David W Li; SUMOylation Regulates Vimentin Functions in Lens. Invest. Ophthalmol. Vis. Sci. 201657(12):.

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      © 2017 Association for Research in Vision and Ophthalmology.

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Abstract

Purpose : Previous studies have shown that mutation of E151K in vimentin leads to cataractogenesis. However, the molecular mechanism remains large unknown. Here we demonstrate that E151K mutation leads to abnormal SUMOylation of vimentin and interferes its polymerization.

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

Results : Wild type and mutant vimentin display differential SUMOylation patterns and thus functional difference.

Conclusions : These results provide explanation why E151K mutation leads to cataractogenesis. (Supported by Research Prevent Blindness, NSFC, Zhongshan Ophthalmic Center, and Chinese Scholarship Council)

This is an abstract that was submitted for the 2016 ARVO Annual Meeting, held in Seattle, Wash., May 1-5, 2016.

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