ArticleNucleic acids research2016
SLIRP stabilizes LRPPRC via an RRM-PPR protein interface.
Article in Nucleic acids research, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 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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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
30 citing papers in PubMed, 1 synthesis or guideline pooled it, 55 citations in OpenAlex.
- LRPPRC: A Multifunctional Protein Involved in Energy Metabolism and Human Disease.Frontiers in physiology · 2019Pooled it
- SLIRP maintains energy metabolism homeostasis in colorectal cancer by stabilizing mitochondrial-encoded mRNAs.British journal of cancer · 2026Article
- Chemical-induced colitis lowers mitochondrial bioenergetic function in colonic tissue with minimal impacts on the proteome.Scientific reports · 2026Article
- SLIRP differentially modulates RNA binding of pathogenic LRPPRC variants.NAR molecular medicine · 2026Article
- Slirp2 modulates oogenesis via regulating mitochondrial protein translation.Journal of molecular cell biology · 2026Article
- Mechanisms at the Intersection of lncRNA and m6A Biology.Non-coding RNA · 2026Review
- Chemical-induced colitis lowers mitochondrial bioenergetic function in the colonic epithelium with minimal impacts on the proteome.Research square · 2025Article
- Targeting COPA to Enhance Erdafitinib Sensitivity in FGFR-Altered Bladder Cancer.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- LINC02154 promotes cell cycle and mitochondrial function in oral squamous cell carcinoma.Cancer science · 2025Article
- Structural basis of LRPPRC-SLIRP-dependent translation by the mitoribosome.Nature structural & molecular biology · 2024Article
- The mitochondrial mRNA-stabilizing protein SLIRP regulates skeletal muscle mitochondrial structure and respiration by exercise-recoverable mechanisms.Nature communications · 2024Article
- LRPPRC and SLIRP synergize to maintain sufficient and orderly mammalian mitochondrial translation.Nucleic acids research · 2024Article
- Sls1 and Mtf2 mediate the assembly of the Mrh5C complex required for activation of cox1 mRNA translation.The Journal of biological chemistry · 2024Article
- Mitochondrial nucleic acids in innate immunity and beyond.Experimental & molecular medicine · 2023Review
- RNA binding protein: coordinated expression between the nuclear and mitochondrial genomes in tumors.Journal of translational medicine · 2023Review
- Article
- Brown adipocyte ATF4 activation improves thermoregulation and systemic metabolism.Cell reports · 2021Article
- Human Mitochondrial RNA Processing and Modifications: Overview.International journal of molecular sciences · 2021Review
- Poly (A) tail length of human mitochondrial mRNAs is tissue-specific and a mutation in LRPPRC results in transcript-specific patterns of deadenylation.Molecular genetics and metabolism reports · 2020Article
- Structural basis of mitochondrial translation.eLife · 2020Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 3 institutions in 4 countries.
Funding
Abstract
LRPPRC is a protein that has attracted interest both for its role in post-transcriptional regulation of mitochondrial gene expression and more recently because numerous mutated variants have been characterized as causing severe infantile mitochondrial neurodegeneration. LRPPRC belongs to the pentatricopeptide repeat (PPR) protein family, originally defined by their RNA binding capacity, and forms a complex with SLIRP that harbours an RNA recognition motif (RRM) domain. We show here that LRPPRC displays a broad and strong RNA binding capacity in vitro in contrast to SLIRP that associates only weakly with RNA. The LRPPRC-SLIRP complex comprises a hetero-dimer via interactions by polar amino acids in the single RRM domain of SLIRP and three neighbouring PPR motifs in the second quarter of LRPPRC, which critically contribute to the LRPPRC-SLIRP binding interface to enhance its stability. Unexpectedly, specific amino acids at this interface are located within the PPRs of LRPPRC at positions predicted to interact with RNA and within the RNP1 motif of SLIRP's RRM domain. Our findings thus unexpectedly establish that despite the prediction that these residues in LRPPRC and SLIRP should bind RNA, they are instead used to facilitate protein-protein interactions, enabling the formation of a stable complex between these two proteins.
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Registered trials
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.