ArticleNature communications2016
Structure of the RBM7-ZCCHC8 core of the NEXT complex reveals connections to splicing factors.
Article in Nature communications, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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Who cites it
35 citing papers in PubMed, 56 citations in OpenAlex.
- RNA-binding proteins in the mouse lens: Functional classifications, expression profiling, and interaction studies of Carhsp1 with crystallin mRNAs.Developmental biology · 2026Article
- PSMA8-Containing 20S Proteasome Regulates Spermiogenesis and Male Fertility.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Defining the roles of the Integrator, NEXT, and nuclear exosome complexes in Drosophila oogenesis.Cell reports · 2025Article
- Enhanced identification of small molecules binding to hnRNPA1 via cryptic pockets mapping coupled with X-Ray fragment screening.bioRxiv : the preprint server for biology · 2024Article
- RNA 3'end tailing safeguards cells against products of pervasive transcription termination.Nature communications · 2024Article
- ZCCHC8 p.P410A disrupts nucleocytoplasmic localization, promoting idiopathic pulmonary fibrosis and chronic obstructive pulmonary disease.Molecular medicine (Cambridge, Mass.) · 2024Article
- RBM7 deficiency promotes breast cancer metastasis by coordinating MFGE8 splicing switch and NF-kB pathway.eLife · 2024Article
- Synergistic action of the Arabidopsis spliceosome components PRP39a and SmD1b in promoting posttranscriptional transgene silencing.The Plant cell · 2023Article
- Maturation of small nucleolar RNAs: from production to function.RNA biology · 2023Review
- C-terminal determinants for RNA binding motif 7 protein stability and RNA recognition.Biophysical chemistry · 2023Article
- MPP6 stimulates both RRP6 and DIS3 to degrade a specified subset of MTR4-sensitive substrates in the human nucleus.Nucleic acids research · 2022Article
- Structure and regulation of the nuclear exosome targeting complex guides RNA substrates to the exosome.Molecular cell · 2022Article
- Structural basis for RNA surveillance by the human nuclear exosome targeting (NEXT) complex.Cell · 2022Article
- Rapid factor depletion highlights intricacies of nucleoplasmic RNA degradation.Nucleic acids research · 2022Article
- The distinct roles of zinc finger CCHC-type (ZCCHC) superfamily proteins in the regulation of RNA metabolism.RNA biology · 2021Review
- The zinc-finger protein Red1 orchestrates MTREC submodules and binds the Mtl1 helicase arch domain.Nature communications · 2021Article
- Genome-wide analysis of CCHC-type zinc finger (ZCCHC) proteins in yeast, Arabidopsis, and humans.Cellular and molecular life sciences : CMLS · 2020Review
- SERRATE interacts with the nuclear exosome targeting (NEXT) complex to degrade primary miRNA precursors in Arabidopsis.Nucleic acids research · 2020Article
- Mapping domains of ARS2 critical for its RNA decay capacity.Nucleic acids research · 2020Article
- Concurrent binding to DNA and RNA facilitates the pluripotency reprogramming activity of Sox2.Nucleic acids research · 2020Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The eukaryotic RNA exosome participates extensively in RNA processing and degradation. In human cells, three accessory factors (RBM7, ZCCHC8 and hMTR4) interact to form the nuclear exosome targeting (NEXT) complex, which directs a subset of non-coding RNAs for exosomal degradation. Here we elucidate how RBM7 is incorporated in the NEXT complex. We identify a proline-rich segment of ZCCHC8 as the interaction site for the RNA-recognition motif (RRM) of RBM7 and present the crystal structure of the corresponding complex at 2.0 Å resolution. On the basis of the structure, we identify a proline-rich segment within the splicing factor SAP145 with strong similarity to ZCCHC8. We show that this segment of SAP145 not only binds the RRM region of another splicing factor SAP49 but also the RRM of RBM7. These dual interactions of RBM7 with the exosome and the spliceosome suggest a model whereby NEXT might recruit the exosome to degrade intronic RNAs.
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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.