ArticleNucleic acids research2019
LARP4A recognizes polyA RNA via a novel binding mechanism mediated by disordered regions and involving the PAM2w motif, revealing interplay between PABP, LARP4A and mRNA.
Article in Nucleic acids research, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed.
- RNA-binding proteins in the mouse lens: Functional classifications, expression profiling, and interaction studies of Carhsp1 with crystallin mRNAs.Developmental biology · 2026Article
- Inhibition of LARP4-mediated quiescence exit of naive CD4Nature biomedical engineering · 2026Article
- An intrinsically disordered region mediates RNA-binding selectivity and cellular activities of LARP6.Nature communications · 2026Article
- Deciphering the RNA recognition by Musashi-1 to design protein and RNA variants for in vitro and in vivo applications.Nucleic acids research · 2025Article
- Noncanonical RNA binding of human La-related protein 6.Nucleic acids research · 2025Article
- Article
- The short conserved region-2 of LARP4 interacts with ribosome-associated RACK1 and promotes translation.Nucleic acids research · 2025Article
- The short conserved region-2 of LARP4 interacts with ribosome-associated RACK1 and promotes translation.bioRxiv : the preprint server for biology · 2024Article
- Genome-wide investigation of the LARP gene family: focus on functional identification and transcriptome profiling of ZmLARP6c1 in maize pollen.BMC plant biology · 2024Article
- The RNA binding proteins LARP4A and LARP4B promote sarcoma and carcinoma growth and metastasis.iScience · 2024Article
- Divergence in regulatory mechanisms of GR-RBP genes in different plants under abiotic stress.Scientific reports · 2024Article
- LARP4 is an RNA-binding protein that binds nuclear-encoded mitochondrial mRNAs to promote mitochondrial function.RNA (New York, N.Y.) · 2024Article
- Enhanced binding of guanylated poly(A) RNA by the LaM domain of LARP1.RNA biology · 2024Article
- La-related protein 4 is enriched in vaccinia virus factories and is required for efficient viral replication in primary human fibroblasts.Microbiology spectrum · 2023Article
- Structure of LARP7 Protein p65-telomerase RNA Complex in Telomerase Revealed by Cryo-EM and NMR.Journal of molecular biology · 2023Article
- La-related protein 4 is enriched in vaccinia virus factories and is required for efficient viral replication in primary human fibroblasts.bioRxiv : the preprint server for biology · 2023Article
- Short poly(A) tails are protected from deadenylation by the LARP1-PABP complex.Nature structural & molecular biology · 2023Article
- Interaction of LARP4 to filamin A mechanosensing domain regulates cell migrations.Frontiers in cell and developmental biology · 2023Article
- The La-related proteins: structures and interactions of a versatile superfamily of RNA-binding proteins.RNA biology · 2021Review
- The LARP1 La-Module recognizes both ends of TOP mRNAs.RNA biology · 2021Article
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11 authors.
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Abstract
LARP4A belongs to the ancient RNA-binding protein superfamily of La-related proteins (LARPs). In humans, it acts mainly by stabilizing mRNAs, enhancing translation and controlling polyA lengths of heterologous mRNAs. These activities are known to implicate its association with mRNA, protein partners and translating ribosomes, albeit molecular details are missing. Here, we characterize the direct interaction between LARP4A, oligoA RNA and the MLLE domain of the PolyA-binding protein (PABP). Our study shows that LARP4A-oligoA association entails novel RNA recognition features involving the N-terminal region of the protein that exists in a semi-disordered state and lacks any recognizable RNA-binding motif. Against expectations, we show that the La module, the conserved RNA-binding unit across LARPs, is not the principal determinant for oligoA interaction, only contributing to binding to a limited degree. Furthermore, the variant PABP-interacting motif 2 (PAM2w) featured in the N-terminal region of LARP4A was found to be important for both RNA and PABP recognition, revealing a new role for this protein-protein binding motif. Our analysis demonstrates the mutual exclusive nature of the PAM2w-mediated interactions, thereby unveiling a tantalizing interplay between LARP4A, polyA and PABP.
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