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J. Biol. Chem., Vol. 283, Issue 10, 6607-6615, March 7, 2008

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A Role for Lengsin, a Recruited Enzyme, in Terminal Differentiation in the Vertebrate Lens^*

From the National Eye Institute, National Institutes of Health, Bethesda, Maryland 20892

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.

Received for publication, November 7, 2007 , and in revised form, January 2, 2008.

^* This work was supported by the Intramural Research Program of the NEI, National Institutes of Health. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

¹ To whom correspondence should be addressed: Section on Molecular Structure and Functional Genomics, National Eye Institute, Bldg. 7, Rm. 201, National Institutes of Health, Bethesda, MD 20892-0703. Tel.: 301-402-3452; Fax: 301-496-0078; E-mail: graeme{at}helix.nih.gov.

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