ArticleMolecular and cellular biology2012
snRNA 3' end formation requires heterodimeric association of integrator subunits.
Article in Molecular and cellular biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.
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Who cites it
47 citing papers in PubMed, 82 citations in OpenAlex.
- Integrator subunit IntS11 orchestrates the temporal dynamics of neural lineage progression in Drosophila.Cell & bioscience · 2026Article
- Defining the roles of the Integrator, NEXT, and nuclear exosome complexes in Drosophila oogenesis.Cell reports · 2025Article
- SUMO conjugation to promoter-proximal sequence elements-associated proteins impacts on snRNA transcription.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- DNA-directed termination of mammalian RNA polymerase II.Genes & development · 2024Article
- Cytoplasmic binding partners of the Integrator endonuclease INTS11 and its paralog CPSF73 are required for their nuclear function.Molecular cell · 2024Article
- Identifying human pre-mRNA cleavage and polyadenylation factors by genome-wide CRISPR screens using a dual fluorescence readthrough reporter.Nucleic acids research · 2024Article
- Decoding the prognostic significance of integrator complex subunit 9 (INTS9) in glioma: links to TP53 mutations, E2F signaling, and inflammatory microenvironments.Cancer cell international · 2023Article
- Bi-allelic variants in INTS11 are associated with a complex neurological disorder.American journal of human genetics · 2023Article
- A combinatorial approach to uncover an additional Integrator subunit.Cell reports · 2023Article
- Genome-wide screening for genetic variants in polyadenylation signal (PAS) sites in mouse selection lines for fatness and leanness.Mammalian genome : official journal of the International Mammalian Genome Society · 2023Article
- Integrator is a global promoter-proximal termination complex.Molecular cell · 2023Review
- Coevolution combined with molecular dynamics simulations provides structural and mechanistic insights into the interactions between the integrator complex subunits.Computational and structural biotechnology journal · 2023Article
- SUMO conjugation regulates the activity of the Integrator complex.Nucleic acids research · 2022Article
- Integrator endonuclease drives promoter-proximal termination at all RNA polymerase II-transcribed loci.Molecular cell · 2022Article
- INTS13 variants causing a recessive developmental ciliopathy disrupt assembly of the Integrator complex.Nature communications · 2022Article
- Inositol hexakisphosphate is required for Integrator function.Nature communications · 2022Article
- BRAT1 links Integrator and defective RNA processing with neurodegeneration.Nature communications · 2022Article
- The 3' Pol II pausing at replication-dependent histone genes is regulated by Mediator through Cajal bodies' association with histone locus bodies.Nature communications · 2022Article
- Who let the DoGs out? - biogenesis of stress-induced readthrough transcripts.Trends in biochemical sciences · 2022Review
- The Integrator complex at the crossroad of coding and noncoding RNA.Current opinion in cell biology · 2021Review
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
The Integrator Complex is a group of proteins responsible for the endonucleolytic cleavage of primary small nuclear RNA (snRNA) transcripts within the nucleus. Integrator subunits 9 and 11 (IntS9/11) are thought to contain the catalytic activity based on their high sequence similarity to CPSF100 and CPSF73, which have been shown to be components of both the poly(A)(+) and histone pre-mRNA cleavage complex. Here we demonstrate that the specific heterodimeric interaction between IntS9 and IntS11 is mediated by a discrete domain present at the extreme C terminus of IntS9 and within the C terminus of IntS11, adjacent to the predicted active site of this endonuclease. This domain is highly conserved within IntS11 but conspicuously absent in CPSF73. Using a cell-based complementation assay that measures Integrator activity, we determined that the IntS9 interaction domain within IntS11 is required for its ability to restore snRNA 3' end processing after RNA interference (RNAi)-mediated depletion of IntS11. Moreover, overexpression of these interaction domains alone elicits snRNA misprocessing through a dominant-negative titration of endogenous Integrator subunits. These data collectively explain the mechanism by which the IntS11/9 and, by analogy, the CPSF73/100 heterodimeric cleavage factors distinguish themselves from each other and demonstrate that the heterodimeric interaction is functionally required for snRNA 3' end formation.
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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.