Evidence map›Paper›PMID 27345150›Full record

ArticleMolecular cell2016

Structure of a Cytoplasmic 11-Subunit RNA Exosome Complex.

Eva Kowalinski, Alexander Kögel, Judith Ebert, Peter Reichelt, Elisabeth Stegmann, Bianca Habermann, Elena Conti

Open access · bronzeAbstract read
In one paragraph

Article in Molecular cell, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.

0numbers the graph read from it
0cells of the map it votes in
58citing papers in PubMed
8.0field-weighted citation impact, top 2% 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

58 citing papers in PubMed, 96 citations in OpenAlex.

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  17. A blood-brain penetrant RNA-targeted small molecule triggers elimination of r(GProceedings of the National Academy of Sciences of the United States of America · 2022
    Article
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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

7 authors at 1 institution in 1 country.

Eva KowalinskiDepartment of Structural Cell Biology, Max Planck Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany.
Alexander KögelDepartment of Structural Cell Biology, Max Planck Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany.
Judith EbertDepartment of Structural Cell Biology, Max Planck Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany.
Peter ReicheltDepartment of Structural Cell Biology, Max Planck Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany.
Elisabeth StegmannDepartment of Structural Cell Biology, Max Planck Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany.
Bianca HabermannComputational Biology, Max Planck Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany.
Elena ContiDepartment of Structural Cell Biology, Max Planck Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany. Electronic address: conti@biochem.mpg.de.
Max Planck Institute of Biochemistry · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The RNA exosome complex associates with nuclear and cytoplasmic cofactors to mediate the decay, surveillance, or processing of a wide variety of transcripts. In the cytoplasm, the conserved core of the exosome (Exo10) functions together with the conserved Ski complex. The interaction of S. cerevisiae Exo10 and Ski is not direct but requires a bridging cofactor, Ski7. Here, we report the 2.65 Å resolution structure of S. cerevisiae Exo10 bound to the interacting domain of Ski7. Extensive hydrophobic interactions rationalize the high affinity and stability of this complex, pointing to Ski7 as a constitutive component of the cytosolic exosome. Despite the absence of sequence homology, cytoplasmic Ski7 and nuclear Rrp6 bind Exo10 using similar surfaces and recognition motifs. Knowledge of the interacting residues in the yeast complexes allowed us to identify a splice variant of human HBS1-Like as a Ski7-like exosome-binding protein, revealing the evolutionary conservation of this cytoplasmic cofactor.

Indexed as

Adaptor Proteins, Signal TransducingAmino Acid SequenceBinding SitesConserved SequenceEvolution, MolecularExosome Multienzyme Ribonuclease ComplexGTP-Binding ProteinsHSP70 Heat-Shock ProteinsHumansHydrophobic and Hydrophilic InteractionsModels, MolecularMutationNuclear ProteinsPeptide Elongation FactorsProtein BindingProtein ConformationAdaptor Proteins, Signal TransducingCSL4 protein, S cerevisiaeExosome Multienzyme Ribonuclease ComplexGTP-Binding ProteinsHBS1L protein, humanHSP70 Heat-Shock ProteinsMTR3 protein, S cerevisiaeNuclear ProteinsPeptide Elongation FactorsProtein IsoformsRRP6 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsSKI7 protein, S cerevisiae

Identifiers

PMID27345150
PMCPMC4942675
OpenAlexW2473423654

What OpenQuestion holds

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LicenceCC BY-NC-ND
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Registered trials

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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.