ArticleNature structural & molecular biology2016
Structural basis and function of XRN2 binding by XTB domains.
Article in Nature structural & molecular biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 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
13 citing papers in PubMed, 21 citations in OpenAlex.
- hnRNPUL1 has a dead polynucleotide kinase domain that regulates RNA and protein interactions.iScience · 2026Article
- Characterization of exoribonuclease XRN1 as a cancer target and identification of adenosine-3',5'-bisphosphate as a potent enzyme inhibitor.Communications biology · 2025Article
- The making and breaking of tRNAs by ribonucleases.Trends in genetics : TIG · 2024Review
- Observation of conformational changes that underlie the catalytic cycle of Xrn2.Nature chemical biology · 2022Article
- Nuclear RNA Regulation by XRN2 and XTBD Family Proteins.Cell structure and function · 2021Review
- A termination-independent role of Rat1 in cotranscriptional splicing.Nucleic acids research · 2021Article
- β-Strand-mediated interactions of protein domains.Proteins · 2020Article
- Full-length NF-κB repressing factor contains an XRN2 binding domain.The Biochemical journal · 2020Article
- IT'S 2 for the price of 1: Multifaceted ITS2 processing machines in RNA and DNA maintenance.DNA repair · 2019Review
- RIF1 promotes tumor growth and cancer stem cell-like traits in NSCLC by protein phosphatase 1-mediated activation of Wnt/β-catenin signaling.Cell death & disease · 2018Article
- Noncoding RNA Surveillance: The Ends Justify the Means.Chemical reviews · 2018Review
- The G-patch protein NF-κB-repressing factor mediates the recruitment of the exonuclease XRN2 and activation of the RNA helicase DHX15 in human ribosome biogenesis.Nucleic acids research · 2017Article
- XRN2 Autoregulation and Control of Polycistronic Gene Expresssion in Caenorhabditis elegans.PLoS genetics · 2016Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
The RNase XRN2 is essential in RNA metabolism. In Caenorhabditis elegans, XRN2 functions with PAXT-1, which shares a putative XRN2-binding domain (XTBD) with otherwise unrelated mammalian proteins. Here, we characterize the structure and function of an XTBD-XRN2 complex. Although XTBD stably interconnects two XRN2 domains through numerous interacting residues, mutation of a single critical residue suffices to disrupt XTBD-XRN2 complexes in vitro and to recapitulate paxt-1-null mutant phenotypes in vivo. Demonstrating conservation of function, vertebrate XTBD-containing proteins bind XRN2 in vitro, and human CDKN2AIPNL (HsC2AIL) can substitute for PAXT-1 in vivo. In vertebrates, which express three distinct XTBD-containing proteins, XRN2 may partition into distinct stable heterodimeric complexes, which probably differ in subcellular localization or function. In C. elegans, complex formation with PAXT-1, the sole XTBD protein, serves to preserve the stability of XRN2 in the absence of substrate.
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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.