ArticleRNA (New York, N.Y.)2009
A comprehensive analysis of the La-motif protein superfamily.
Article in RNA (New York, N.Y.), 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 116 papers, 1 of them a synthesis that pooled it.
What it found
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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
116 citing papers in PubMed, 1 synthesis or guideline pooled it, 199 citations in OpenAlex.
- PABPC1--mRNA stability, protein translation and tumorigenesis.Frontiers in oncology · 2022Pooled it
- La1: an evolutionarily conserved player in the Arabidopsis telomerase complex.Plant cell reports · 2026Article
- RNA-binding protein LARP6 coordinates hepatic stellate cell activation and liver fibrosis.The Journal of clinical investigation · 2026Article
- Review
- The LARP6 La module fromRNA biology · 2025Article
- Noncanonical RNA binding of human La-related protein 6.Nucleic acids research · 2025Article
- Key RNA-binding domains in the La protein establish tRNA modification levels in Trypanosoma brucei.Nucleic acids research · 2025Article
- Article
- A Robust Expression and Purification Protocol for the Production of the La Domain of Human LARP6.ACS omega · 2025Article
- Genome-Wide Association Study on Cowpea seed coat color using RGB images.Molecular breeding : new strategies in plant improvement · 2024Article
- LARP1 binds ribosomes and TOP mRNAs in repressed complexes.The EMBO journal · 2024Article
- Article
- 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
- LARP4 is an RNA-binding protein that binds nuclear-encoded mitochondrial mRNAs to promote mitochondrial function.RNA (New York, N.Y.) · 2024Article
- Comparative analysis of the LARP1 C-terminal DM15 region through Coelomate evolution.PloS one · 2024Article
- Enhanced binding of guanylated poly(A) RNA by the LaM domain of LARP1.RNA biology · 2024Article
- LARP1 senses free ribosomes to coordinate supply and demand of ribosomal proteins.bioRxiv : the preprint server for biology · 2023Article
- NMR Analysis Suggests Synergy between the RRM2 and the Carboxy-Terminal Segment of Human La Protein in the Recognition and Interaction with HCV IRES.International journal of molecular sciences · 2023Article
- LARP6 suppresses colorectal cancer progression through ZNF267/SGMS2-mediated imbalance of sphingomyelin synthesis.Journal of experimental & clinical cancer research : CR · 2023Article
56 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The extremely well-conserved La motif (LAM), in synergy with the immediately following RNA recognition motif (RRM), allows direct binding of the (genuine) La autoantigen to RNA polymerase III primary transcripts. This motif is not only found on La homologs, but also on La-related proteins (LARPs) of unrelated function. LARPs are widely found amongst eukaryotes and, although poorly characterized, appear to be RNA-binding proteins fulfilling crucial cellular functions. We searched the fully sequenced genomes of 83 eukaryotic species scattered along the tree of life for the presence of LAM-containing proteins. We observed that these proteins are absent from archaea and present in all eukaryotes (except protists from the Plasmodium genus), strongly suggesting that the LAM is an ancestral motif that emerged early after the archaea-eukarya radiation. A complete evolutionary and structural analysis of these proteins resulted in their classification into five families: the genuine La homologs and four LARP families. Unexpectedly, in each family a conserved domain representing either a classical RRM or an RRM-like motif immediately follows the LAM of most proteins. An evolutionary analysis of the LAM-RRM/RRM-L regions shows that these motifs co-evolved and should be used as a single entity to define the functional region of interaction of LARPs with their substrates. We also found two extremely well conserved motifs, named LSA and DM15, shared by LARP6 and LARP1 family members, respectively. We suggest that members of the same family are functional homologs and/or share a common molecular mode of action on different RNA baits.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.