ArticleNucleic acids research2020
The human ZC3H3 and RBM26/27 proteins are critical for PAXT-mediated nuclear RNA decay.
Article in Nucleic acids research, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.
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Who cites it
63 citing papers in PubMed, 84 citations in OpenAlex.
- Review
- Review
- The PAXT connection is a modifier of rare codon-enriched protein expression.Nature communications · 2026Article
- Mechanisms of transcription termination across the coding and noncoding loci of the genome.Nature reviews. Molecular cell biology · 2026Review
- Precision in RNA degradation: helicases, ribosome and RNA polymerase stalling, and RNA modifications.Trends in cell biology · 2026Review
- Review
- Article
- Comprehensive analysis of the RBP regulome reveals functional modules and drug candidates in liver cancer.Scientific reports · 2026Article
- Targeting of the nuclear RNA exosome to chromatin by HP1 affects the transcriptional programs of liver cells.Nature communications · 2026Article
- Identification of immune-related targets of N6-methyladenosine regulators in hepatocellular carcinoma via RNA-seq analysis.Translational cancer research · 2026Article
- Article
- Genome-wide association study meta-analysis identifies susceptibility loci informing Ewing sarcoma etiology and potential mechanisms of risk.medRxiv : the preprint server for health sciences · 2026Article
- Direct coupling of the human nuclear exosome adaptors NEXT and PAXT with transcription termination and processing machineries.Nucleic acids research · 2026Article
- Article
- Multimodal Analysis Reveals Immune Suppression Associated With Hepatocellular Carcinoma Related to RBM27 and Constructs a Prognostic Model.Human mutation · 2026Article
- Nuclear effects play an important role in determining codon usage-dependent human gene expression.Nature communications · 2025Article
- EXOSC3 S1-domain variants implicated in PCH1b alter RNA exosome cap subunit abundance and thermal stability disrupting rRNA processing and targeting of AU-rich mRNA.bioRxiv : the preprint server for biology · 2025Article
- The nuclear exosome co-factor MTR4 shapes the transcriptome for meiotic initiation.Nature communications · 2025Article
- Article
- Antagonistic roles by the conserved nuclear poly(A)-binding proteins PABPN1 and ZC3H14 in nuclear RNA surveillance.Nucleic acids research · 2025Article
3 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
12 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Recruitment of the human ribonucleolytic RNA exosome to nuclear polyadenylated (pA+) RNA is facilitated by the Poly(A) Tail eXosome Targeting (PAXT) connection. Besides its core dimer, formed by the exosome co-factor MTR4 and the ZFC3H1 protein, the PAXT connection remains poorly defined. By characterizing nuclear pA+-RNA bound proteomes as well as MTR4-ZFC3H1 containing complexes in conditions favoring PAXT assembly, we here uncover three additional proteins required for PAXT function: ZC3H3, RBM26 and RBM27 along with the known PAXT-associated protein, PABPN1. The zinc-finger protein ZC3H3 interacts directly with MTR4-ZFC3H1 and loss of any of the newly identified PAXT components results in the accumulation of PAXT substrates. Collectively, our results establish new factors involved in the turnover of nuclear pA+ RNA and suggest that these are limiting for PAXT activity.
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