Evidence map›Paper›PMID 37889751›Full record

ArticleCell reports2023

Dual agonistic and antagonistic roles of ZC3H18 provide for co-activation of distinct nuclear RNA decay pathways.

Patrik Polák, William Garland, Om Rathore, Manfred Schmid, Anna Salerno-Kochan, Lis Jakobsen, Maria Gockert, Piotr Gerlach, Toomas Silla, Jens S Andersen and 2 more

Open access · goldAbstract read
In one paragraph

Article in Cell reports, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
2.8field-weighted citation impact, top 9% 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

15 citing papers in PubMed, 18 citations in OpenAlex.

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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

12 authors at 3 institutions in 2 countries.

Patrik PolákDepartment of Molecular Biology and Genetics, Universitetsbyen 81, Aarhus University, Aarhus, Denmark.
William GarlandDepartment of Molecular Biology and Genetics, Universitetsbyen 81, Aarhus University, Aarhus, Denmark.
Om RathoreDepartment of Molecular Biology and Genetics, Universitetsbyen 81, Aarhus University, Aarhus, Denmark.
Manfred SchmidDepartment of Molecular Biology and Genetics, Universitetsbyen 81, Aarhus University, Aarhus, Denmark.
Anna Salerno-KochanDepartment of Structural Cell Biology, Max Planck Institute of Biochemistry, Am Klopferspitz 18, Martinsried/Munich, Germany.
Lis JakobsenDepartment of Biochemistry and Molecular Biology, University of Southern Denmark, Campusvej 55, Odense M, Denmark.
Maria GockertDepartment of Molecular Biology and Genetics, Universitetsbyen 81, Aarhus University, Aarhus, Denmark.
Piotr GerlachDepartment of Structural Cell Biology, Max Planck Institute of Biochemistry, Am Klopferspitz 18, Martinsried/Munich, Germany.
Toomas SillaDepartment of Molecular Biology and Genetics, Universitetsbyen 81, Aarhus University, Aarhus, Denmark.
Jens S AndersenDepartment of Biochemistry and Molecular Biology, University of Southern Denmark, Campusvej 55, Odense M, Denmark.
Elena ContiDepartment of Structural Cell Biology, Max Planck Institute of Biochemistry, Am Klopferspitz 18, Martinsried/Munich, Germany.
Torben Heick JensenDepartment of Molecular Biology and Genetics, Universitetsbyen 81, Aarhus University, Aarhus, Denmark. Electronic address: thj@mbg.au.dk.
Aarhus University · DKMax Planck Institute of Biochemistry · DEUniversity of Southern Denmark · DK

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The RNA exosome is a versatile ribonuclease. In the nucleoplasm of mammalian cells, it is assisted by its adaptors the nuclear exosome targeting (NEXT) complex and the poly(A) exosome targeting (PAXT) connection. Via its association with the ARS2 and ZC3H18 proteins, NEXT/exosome is recruited to capped and short unadenylated transcripts. Conversely, PAXT/exosome is considered to target longer and adenylated substrates via their poly(A) tails. Here, mutational analysis of the core PAXT component ZFC3H1 uncovers a separate branch of the PAXT pathway, which targets short adenylated RNAs and relies on a direct ARS2-ZFC3H1 interaction. We further demonstrate that similar acidic-rich short linear motifs of ZFC3H1 and ZC3H18 compete for a common ARS2 epitope. Consequently, while promoting NEXT function, ZC3H18 antagonizes PAXT activity. We suggest that this organization of RNA decay complexes provides co-activation of NEXT and PAXT at loci with abundant production of short exosome substrates.

Indexed as

RNA-Binding ProteinsRNA, NuclearAnimalsCell NucleusExosome Multienzyme Ribonuclease ComplexMammalsRNA, MessengerRNA StabilityExosome Multienzyme Ribonuclease ComplexRNA-Binding ProteinsRNA, MessengerRNA, NuclearactivationARS2CP: Molecular biologyinhibitionNEXTnuclear RNA decayPAXTZC3H18

Identifiers

PMID37889751
PMCPMC10720265
OpenAlexW4387961272

What OpenQuestion holds

Textmetadata
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.