May 2008
Volume 49, Issue 13
Free
ARVO Annual Meeting Abstract  |   May 2008
Lengsin, a Recruited Enzyme, Associates With Cytoskeleton in Lens Fiber Cell Terminal Differentiation
Author Affiliations & Notes
  • G. J. Wistow
    National Eye Inst/NIH, Bethesda, Maryland
  • K. Wyatt
    National Eye Inst/NIH, Bethesda, Maryland
  • C. Gao
    National Eye Inst/NIH, Bethesda, Maryland
  • J.-Y. Tsai
    National Eye Inst/NIH, Bethesda, Maryland
  • R. Fariss
    National Eye Inst/NIH, Bethesda, Maryland
  • S. Ray
    National Eye Inst/NIH, Bethesda, Maryland
  • C. Slingsby
    Birkbeck College, London, United Kingdom
  • E. Orlova
    Birkbeck College, London, United Kingdom
  • L. Dong
    National Eye Inst/NIH, Bethesda, Maryland
  • Footnotes
    Commercial Relationships  G.J. Wistow, None; K. Wyatt, None; C. Gao, None; J. Tsai, None; R. Fariss, None; S. Ray, None; C. Slingsby, None; E. Orlova, None; L. Dong, None.
  • Footnotes
    Support  NEI Intramural:MRC
Investigative Ophthalmology & Visual Science May 2008, Vol.49, 1526. doi:https://doi.org/
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      G. J. Wistow, K. Wyatt, C. Gao, J.-Y. Tsai, R. Fariss, S. Ray, C. Slingsby, E. Orlova, L. Dong; Lengsin, a Recruited Enzyme, Associates With Cytoskeleton in Lens Fiber Cell Terminal Differentiation. Invest. Ophthalmol. Vis. Sci. 2008;49(13):1526. doi: https://doi.org/.

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

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Abstract

Purpose: : To investigate the structure and function of Lengsin, a recently discovered major protein of the vertebrate eye lens.

Methods: : Recombinant protein expression, yeast 2-hybrid analysis, surface plasmon resonance, electron microscopy, immunofluorescence, ‘knock out’ mouse.

Results: : Lengsin is lens-specific and highly conserved in vertebrate evolution, although it also shows taxon-specific differences in exon usage. It is a member of a family of class I glutamine synthetases (GS) with a 12-mer structure similar to that of prokaryotic GS but has lost enzyme function. Lengsin is expressed in terminally differentiating secondary lens fiber cells in adult lens. It can bind the lens intermediate filament proteins vimentin and CP49 and localizes with them at the fiber cell plasma membrane. Co-expressed lengsin and a filament region of vimentin associate in solution and are being examined for complex structure by CryoEM. The Lengsin gene has been deleted in mice and preliminary observations suggest defects in fiber cell packing.

Conclusions: : Lengsin is a lone vertebrate survivor of an ancient group of enzymes. It appears to have been recruited to a highly specialized structural role in the lens in which its expression marks the terminal differentiation of secondary fiber cells. Lengsin associates with lens intermediate filament proteins, including beaded filaments, suggesting that it may be involved in organizing the architecture of fiber cells as they lose organelles and form tightly interdigitated cell contacts.

Keywords: protein structure/function • cytoskeleton 
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