Evidence map›Paper›PMID 29274231›Full record

ArticleeLife2017

Structural insights into the assembly and polyA signal recognition mechanism of the human CPSF complex.

Marcello Clerici, Marco Faini, Ruedi Aebersold, Martin Jinek

Open access · goldAbstract read
In one paragraph

Article in eLife, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.

0numbers the graph read from it
0cells of the map it votes in
60citing papers in PubMed
4.1field-weighted citation impact, top 5% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

The trial behind it

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.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

60 citing papers in PubMed, 88 citations in OpenAlex.

  1. Review
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  5. Poly(A) tail regulation in stem cells and early development.Cell regeneration (London, England) · 2025
    Review
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors at 2 institutions in 1 country.

Marcello ClericiDepartment of Biochemistry, University of Zurich, Zurich, Switzerland.ORCID http://orcid.org/0000-0003-2906-0982
Marco FainiDepartment of Biology, Institute of Molecular Systems Biology, ETH Zurich, Zurich, Switzerland.ORCID http://orcid.org/0000-0001-8131-7648
Ruedi AebersoldDepartment of Biology, Institute of Molecular Systems Biology, ETH Zurich, Zurich, Switzerland.
Martin JinekDepartment of Biochemistry, University of Zurich, Zurich, Switzerland.ORCID http://orcid.org/0000-0002-7601-210X
University of Zurich · CHETH Zurich · CH

Funding

European Research Council 233226European Research Council 670821
6 · The paper itself

Abstract

3' polyadenylation is a key step in eukaryotic mRNA biogenesis. In mammalian cells, this process is dependent on the recognition of the hexanucleotide AAUAAA motif in the pre-mRNA polyadenylation signal by the cleavage and polyadenylation specificity factor (CPSF) complex. A core CPSF complex comprising CPSF160, WDR33, CPSF30 and Fip1 is sufficient for AAUAAA motif recognition, yet the molecular interactions underpinning its assembly and mechanism of PAS recognition are not understood. Based on cross-linking-coupled mass spectrometry, crystal structure of the CPSF160-WDR33 subcomplex and biochemical assays, we define the molecular architecture of the core human CPSF complex, identifying specific domains involved in inter-subunit interactions. In addition to zinc finger domains in CPSF30, we identify using quantitative RNA-binding assays an N-terminal lysine/arginine-rich motif in WDR33 as a critical determinant of specific AAUAAA motif recognition. Together, these results shed light on the function of CPSF in mediating PAS-dependent RNA cleavage and polyadenylation.

Indexed as

Cleavage And Polyadenylation Specificity FactorCrystallography, X-RayHumansHydrolysisMass SpectrometrymRNA Cleavage and Polyadenylation FactorsNuclear ProteinsPolyadenylationProtein BindingProtein Interaction Domains and MotifsRNA PrecursorsCleavage And Polyadenylation Specificity FactorCPSF4 protein, humanFIP1L1 protein, humanmRNA Cleavage and Polyadenylation FactorsNuclear ProteinsRNA PrecursorsWDR33 protein, humanbiochemistrybiophysicshumanmass spectrometrymRNApolyadenylationprotein-RNA interactionsRNA processingstructural biologyX-ray crystallography

Identifiers

PMID29274231
PMCPMC5760199
OpenAlexW2778462241

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

Registered trials

None linked

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.