Evidence map›Paper›PMID 20139071›Full record

ArticleThe Journal of biological chemistry2010

Cul8/Rtt101 forms a variety of protein complexes that regulate DNA damage response and transcriptional silencing.

Satoru Mimura, Tsuyoshi Yamaguchi, Satoru Ishii, Emiko Noro, Tomoya Katsura, Chikashi Obuse, Takumi Kamura

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
–field-weighted citation impact
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

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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

34 citing papers in PubMed.

  1. Review
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  8. The Ubiquitin-like Proteins ofBiomolecules · 2023
    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

7 authors.

Satoru MimuraDivision of Biological Science, Graduate School of Science, Nagoya University Chikusa-ku, Nagoya 464-8602.
Tsuyoshi YamaguchiDivision of Biological Science, Graduate School of Science, Nagoya University Chikusa-ku, Nagoya 464-8602.
Satoru IshiiDivision of Biological Science, Graduate School of Science, Nagoya University Chikusa-ku, Nagoya 464-8602.
Emiko NoroFaculty of Advanced Life Science, Hokkaido University, Kita-21, Nishi-11, Sapporo, Hokkaido 001-0021, Japan.
Tomoya KatsuraDivision of Biological Science, Graduate School of Science, Nagoya University Chikusa-ku, Nagoya 464-8602.
Chikashi ObuseFaculty of Advanced Life Science, Hokkaido University, Kita-21, Nishi-11, Sapporo, Hokkaido 001-0021, Japan.
Takumi KamuraDivision of Biological Science, Graduate School of Science, Nagoya University Chikusa-ku, Nagoya 464-8602. Electronic address: z47617a@nucc.cc.nagoya-u.ac.jp.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The budding yeast, Saccharomyces cerevisiae, has three cullin proteins, which act as platforms for Cullin-based E3 ubiquitin ligases. Genetic evidence indicates that Cul8, together with Mms1, Mms22, and Esc4, is involved in the repair of DNA damage that can occur during DNA replication. Cul8 is thought to form a complex with these proteins, but the composition and the function of Cul8-based E3 ubiquitin ligases remain largely uncharacterized. Herein, we report a comprehensive biochemical analysis of Cul8 complexes. Cul8 was found to form a Cul8-Mms1-Mms22-Esc4 complex under physiological conditions, with Mms1 bridging Cul8 and Mms22 and Mms22 bridging Mms1 and Esc4. Domain analysis demonstrated that the N-terminal region of Mms1 and the C-terminal region of Mms22 are required for the Mms1-Mms22 interaction, whereas the N-terminal region of Mms22 is required for the Mms22-Esc4 interaction. We also found other Cul8-Mms1-binding proteins Ctf4, Esc2, and Orc5 using yeast two-hybrid screening. Esc4 and Ctf4 bound to Mms22 directly and bound to Cul8-Mms1 in the presence of Mms22, whereas Esc2 and Orc5 interacted with both Cul8 and Mms1, independently. We found that Cul8, Mms1, and Mms22 participated in the regulation of transcriptional silencing of yeast telomeres. These results suggest that Cul8-Mms1, as part of various protein complexes, is involved in the regulation of chromatin metabolism.

Indexed as

DNA DamageGene Expression Regulation, FungalTranscription, GeneticChromatinCullin ProteinsDNA-Binding ProteinsGene SilencingModels, BiologicalProtein BindingSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTelomereTwo-Hybrid System TechniquesChromatinCTF4 protein, S cerevisiaeCullin ProteinsDNA-Binding ProteinsMms1 protein, S cerevisiaeMms22 protein, S cerevisiaeRTT101 protein, S cerevisiaeSaccharomyces cerevisiae Proteins

Identifiers

PMID20139071
PMCPMC2843234

What OpenQuestion holds

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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.