ArticleRNA (New York, N.Y.)2013
The association of a La module with the PABP-interacting motif PAM2 is a recurrent evolutionary process that led to the neofunctionalization of La-related proteins.
Article in RNA (New York, N.Y.), 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
33 citing papers in PubMed, 56 citations in OpenAlex.
- Genome-Wide Identification of LCY Genes inPlants (Basel, Switzerland) · 2026Article
- The LARP6 La module fromRNA biology · 2025Article
- Key RNA-binding domains in the La protein establish tRNA modification levels in Trypanosoma brucei.Nucleic acids research · 2025Article
- 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
- Enhanced binding of guanylated poly(A) RNA by the LaM domain of LARP1.RNA biology · 2024Article
- Short poly(A) tails are protected from deadenylation by the LARP1-PABP complex.Nature structural & molecular biology · 2023Article
- LARP6C orchestrates posttranscriptional reprogramming of gene expression during hydration to promote pollen tube guidance.The Plant cell · 2021Article
- Article
- La proteins couple use of sequence-specific and non-specific binding modes to engage RNA substrates.RNA biology · 2021Review
- The La-related proteins: structures and interactions of a versatile superfamily of RNA-binding proteins.RNA biology · 2021Review
- Review
- Structural dynamics in the La-module of La-related proteins.RNA biology · 2021Article
- LARP1 and LARP4: up close with PABP for mRNA 3' poly(A) protection and stabilization.RNA biology · 2021Review
- A Maize Male Gametophyte-Specific Gene Encodes ZmLARP6c1, a Potential RNA-Binding Protein Required for Competitive Pollen Tube Growth.Frontiers in plant science · 2021Article
- Core spliceosomal Sm proteins as constituents of cytoplasmic mRNPs in plants.The Plant journal : for cell and molecular biology · 2020Article
- TOP mRNPs: Molecular Mechanisms and Principles of Regulation.Biomolecules · 2020Review
- Crystal Structure of a Variant PAM2 Motif of LARP4B Bound to the MLLE Domain of PABPC1.Biomolecules · 2020Article
- Maternal Larp6 controls oocyte development, chorion formation and elevation.Development (Cambridge, England) · 2020Article
- Up-regulation of circ_LARP4 suppresses cell proliferation and migration in ovarian cancer by regulating miR-513b-5p/LARP4 axis.Cancer cell international · 2020Article
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 2 countries.
Funding
Abstract
La-related proteins (LARPs) are largely uncharacterized factors, well conserved throughout evolution. Recent reports on the function of human LARP4 and LARP6 suggest that these proteins fulfill key functions in mRNA metabolism and/or translation. We report here a detailed evolutionary history of the LARP4 and 6 families in eukaryotes. Genes coding for LARP4 and 6 were duplicated in the common ancestor of the vertebrate lineage, but one LARP6 gene was subsequently lost in the common ancestor of the eutherian lineage. The LARP6 gene was also independently duplicated several times in the vascular plant lineage. We observed that vertebrate LARP4 and plant LARP6 duplication events were correlated with the acquisition of a PABP-interacting motif 2 (PAM2) and with a significant reorganization of their RNA-binding modules. Using isothermal titration calorimetry (ITC) and immunoprecipitation methods, we show that the two plant PAM2-containing LARP6s (LARP6b and c) can, indeed, interact with the major plant poly(A)-binding protein (PAB2), while the third plant LARP6 (LARP6a) is unable to do so. We also analyzed the RNA-binding properties and the subcellular localizations of the two types of plant LARP6 proteins and found that they display nonredundant characteristics. As a whole, our results support a model in which the acquisition by LARP4 and LARP6 of a PAM2 allowed their targeting to mRNA 3' UTRs and led to their neofunctionalization.
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