Evidence map›Paper›PMID 25914052›Full record

ArticleStructure (London, England : 1993)2015

Architecture of the ubiquitylation module of the yeast Ccr4-Not complex.

Varun Bhaskar, Jérôme Basquin, Elena Conti

Open access · hybridAbstract read
In one paragraph

Article in Structure (London, England : 1993), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
2.7field-weighted citation impact, top 10% 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

28 citing papers in PubMed, 41 citations in OpenAlex.

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  13. ThePlant physiology · 2020
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  18. RNA (New York, N.Y.) · 2018
    Article
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  20. Mutations in theFrontiers in genetics · 2017
    Article
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

3 authors at 1 institution in 1 country.

Varun BhaskarDepartment of Structural Cell Biology, Max-Planck-Institute of Biochemistry, Am Klopferspitz 18, 82152 Munich, Germany.
Jérôme BasquinDepartment of Structural Cell Biology, Max-Planck-Institute of Biochemistry, Am Klopferspitz 18, 82152 Munich, Germany.
Elena ContiDepartment of Structural Cell Biology, Max-Planck-Institute of Biochemistry, Am Klopferspitz 18, 82152 Munich, 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 Ccr4-Not complex regulates eukaryotic gene expression at multiple levels, including mRNA turnover, translational repression, and transcription. We have studied the ubiquitylation module of the yeast Ccr4-Not complex and addressed how E3 ligase binds cognate E2 and how it is tethered to the complex. The 2.8-Å resolution crystal structure of the N-terminal RING domain of Not4 in complex with Ubc4 shows the detailed interactions of this E3-E2 complex. The 3.6-Å resolution crystal structure of the C-terminal domain of the yeast Not4 in complex with the C-terminal domain of Not1 reveals how a largely extended region at the C-terminus of Not4 wraps around a HEAT-repeat region of Not1. This C-terminal region of Not4 is only partly conserved in metazoans, rationalizing its weaker Not1-binding properties. The structural and biochemical data show how Not1 can incorporate both the ubiquitylation module and the Not2-Not3/5 module concomitantly in the Ccr4-Not complex.

Indexed as

Amino Acid SequenceCell Cycle ProteinsConserved SequenceCrystallography, X-RayModels, MolecularProtein BindingProtein MultimerizationProtein Structure, SecondaryRepressor ProteinsRibonucleasesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTranscription FactorsUbiquitinationUbiquitin-Conjugating EnzymesUbiquitin-Protein LigasesCCR4 protein, S cerevisiaeCDC36 protein, S cerevisiaeCDC39 protein, S cerevisiaeCell Cycle ProteinsMOT2 protein, S cerevisiaeRepressor ProteinsRibonucleasesSaccharomyces cerevisiae ProteinsTranscription FactorsUbc4 protein, S cerevisiaeUbiquitin-Conjugating EnzymesUbiquitin-Protein Ligases

Identifiers

PMID25914052
PMCPMC4431670
OpenAlexW2036540971

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.