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Significance Lens transparency critically requires the abundant accumulation of crystallin proteins, and deregulation of this process causes congenital cataracts in humans. Rbm24 is an RNA-binding protein with highly conserved expression in differentiating lens fiber cells among all vertebrates. We use a zebrafish model to demonstrate that loss of Rbm24 function specifically impedes lens fiber cell differentiation, resulting in cataract formation and blindness. Molecular analyses reveal that Rbm24 interacts with cytoplasmic polyadenylation complex and binds to a large number of lens-expressed messenger RNAs to maintain their stability and protect their poly(A) tail length, thereby crucially contributing to their efficient translation into functional proteins. This work identifies an important mechanism by which Rbm24 posttranscriptionally controls lens gene expression to establish transparency and refraction power.

Rbm24 controls poly(A) tail length and translation efficiency of crystallin mRNAs in the lens via cytoplasmic polyadenylation