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The LARP1 RRM functions as a ribosome responsive regulator of TOP mRNAs

James A Saba, Phoebe E White, A Maxwell Burroughs

    Biorxiv : the Preprint Server for Biology
    |April 27, 2026
    PubMed

    Insights

    La-related protein 1 (LARP1) binds ribosomes to repress messenger RNAs (mRNAs) encoding ribosomal proteins. This ribosome-sensing mechanism, orchestrated by LARP1

    Area of Science:

    • Molecular Biology
    • Cell Biology
    • Biochemistry

    Background:

    • Ribosome synthesis is crucial in metazoans, with dysregulation linked to disease.
    • La-related protein 1 (LARP1) binds inactive ribosomes and represses Terminal OligoPyrimidine (TOP) mRNAs.
    • The mechanistic link between LARP1's ribosome and TOP mRNA binding is unclear.

    Purpose of the Study:

    • To elucidate the mechanistic link between LARP1's ribosome binding and TOP mRNA repression.
    • To investigate the role of LARP1's domains in coordinating these activities.
    • To understand how LARP1 senses cellular ribosome demand.

    Main Methods:

    • In vitro biochemical assays to study LARP1 domain interactions and ribosome binding.
    • Cellular experiments to assess the requirement of ribosome binding for TOP repression.
    • Mutagenesis studies to disrupt LARP1 domain architecture and evaluate cellular effects.

    Main Results:

    • Ribosome binding is essential for LARP1-mediated TOP repression.
    • LARP1's ribosome binding region is part of a novel RNA recognition motif (RRM) domain that interacts with its HEAT repeat domain.
    • Ribosome binding, mediated by RRM unfolding and remodeling, is sufficient in vitro and required in cells for LARP1 to repress and stabilize TOPs.

    Conclusions:

    • LARP1 possesses a ribosome-sensing function coordinated by its RRM domain.
    • This mechanism tunes ribosomal protein synthesis to cellular ribosome demand.
    • Disruption of LARP1's coordinated domain architecture compromises cell fitness.

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