June 2017
Volume 58, Issue 8
Open Access
ARVO Annual Meeting Abstract  |   June 2017
SUMOylation Inhibits E151K Vimentin Function by Interfering with Its Polymerization
Author Affiliations & Notes
  • Ling Wang
    Ophthalmology, University of Nebraska Medical Center, Omaha, Nebraska, United States
    College of Life Sciences, Hunan Normal University, Changsha, Hunan Province, China
  • Xiao-Dong Gong
    College of Life Sciences, Hunan Normal University, Changsha, Hunan Province, China
  • Zhao-Xia Huang
    Ophthalmology, University of Nebraska Medical Center, Omaha, Nebraska, United States
    College of Life Sciences, Hunan Normal University, Changsha, Hunan Province, China
  • Qian Nie
    College of Life Sciences, Hunan Normal University, Changsha, Hunan Province, China
  • James W Gigantelli
    Ophthalmology, University of Nebraska Medical Center, Omaha, Nebraska, United States
  • Quan Dong Nguyen
    Ophthalmology, University of Nebraska Medical Center, Omaha, Nebraska, United States
  • David W Li
    Ophthalmology, University of Nebraska Medical Center, Omaha, Nebraska, United States
    College of Life Sciences, Hunan Normal University, Changsha, Hunan Province, China
  • Footnotes
    Commercial Relationships   Ling Wang, None; Xiao-Dong Gong, None; Zhao-Xia Huang, None; Qian Nie, None; James Gigantelli, None; Quan Nguyen, None; David Li, None
  • Footnotes
    Support   NSFC-81570824
Investigative Ophthalmology & Visual Science June 2017, Vol.58, 1707. doi:
  • Views
  • Share
  • Tools
    • Alerts
      ×
      This feature is available to Subscribers Only
      Sign In or Create an Account ×
    • Get Citation

      Ling Wang, Xiao-Dong Gong, Zhao-Xia Huang, Qian Nie, James W Gigantelli, Quan Dong Nguyen, David W Li; SUMOylation Inhibits E151K Vimentin Function by Interfering with Its Polymerization. Invest. Ophthalmol. Vis. Sci. 2017;58(8):1707.

      Download citation file:


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

      ×
  • Supplements
Abstract

Purpose : It is well established that the E151K mutation in vimentin leads to cataractogenesis. However, the molecular mechanism for this pathogenesis remains large unknown. Here we present evidence to show 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 : These results provide the molecular basis why E151K mutation leads to cataractogenesis. (Supported by Research Prevent Blindness, NSFC-81570824, Zhongshan Ophthalmic Center, and Chinese Scholarship Council)

This is an abstract that was submitted for the 2017 ARVO Annual Meeting, held in Baltimore, MD, May 7-11, 2017.

×
×

This PDF is available to Subscribers Only

Sign in or purchase a subscription to access this content. ×

You must be signed into an individual account to use this feature.

×