A role for lengsin, a recruited enzyme, in terminal differentiation in the vertebrate lens

The Journal of Biological Chemistry
Keith WyattGraeme Wistow

Abstract

Lengsin is an eye lens-specific member of the glutamine synthetase (GS) superfamily. Lengsin has no GS activity, suggesting that it has a structural rather than catalytic role in lens. In situ hybridization and immunofluorescence showed that lengsin is expressed in terminally differentiating secondary lens fiber cells. Yeast two-hybrid (Y2H) and recombinant protein experiments showed that full-length lengsin can bind the 2B filament region of vimentin. In affinity chromatography, lengsin also bound the equivalent region of CP49 (BFSP2; phakinin), a related intermediate filament protein specific to the lens. Both the vimentin and CP49 2B fragments bound lengsin in surface plasmon resonance spectroscopy with fast association and slow dissociation kinetics. Lengsin expression correlates with a transition zone in maturing lens fiber cells in which cytoskeleton is reorganized. Lengsin and lens intermediate filament proteins co-localize at the plasma membrane in maturing fiber cells. This suggests that lengsin may act as a component of the cytoskeleton itself or as a chaperone for the reorganization of intermediate filament proteins during terminal differentiation in the lens.

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Citations

Mar 10, 2009·The Journal of Biological Chemistry·Alicia De MariaSteven Bassnett
Jul 10, 2009·The Journal of Clinical Investigation·Shuhua SongRoy A Quinlan
May 22, 2013·Proteome Science·Sebastian AretzJürgen Kopitz
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Sep 16, 2017·PLoS Genetics·Emily L ClarkDavid A Hume
Sep 24, 2021·Investigative Ophthalmology & Visual Science·Zhen WangKevin L Schey

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