Evidence map›Paper›PMID 18202552›Full record

ArticleCell cycle (Georgetown, Tex.)2008

Yeast Chfr homologs retard cell cycle at G1 and G2/M via Ubc4 and Ubc13/Mms2-dependent ubiquitination.

Greta L Loring, Kathryn C Christensen, Scott A Gerber, Charles Brenner

Open access · bronzeAbstract readComparative Study
In one paragraph

Article in Cell cycle (Georgetown, Tex.), 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
2.0field-weighted citation impact, top 15% 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

19 citing papers in PubMed, 33 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

4 authors at 1 institution in 1 country.

Greta L LoringDepartment of Genetics and Norris Cotton Cancer Center, Dartmouth Medical School, Lebanon, New Hampshire 03756, USA.
Kathryn C Christensen
Scott A Gerber
Charles Brenner
Dartmouth College · US

Funding

Translational Engineering in Cancer (TEC)P30CA023108 · NCI · DARTMOUTH COLLEGE · PI Steven D Leach · 1985 to 2026
$91.3M
THE ROLE OF CAL IN CIF-MEDIATED DEGRADATION OF CFTRP20RR018787 · NCRR · DARTMOUTH COLLEGE · PI O'TOOLE, GEORGE A. · 2003 to 2011
$21.9M
Cancer Biology and Molecular TherapeuticsT32CA009658 · NCI · DARTMOUTH COLLEGE · PI EASTMAN, ALAN R · 1991 to 2011
$3.8M
Quantitative Analysis of RING E3 Ubiquitin LigasesR01GM081665 · NIGMS · UNIVERSITY OF IOWA · PI BRENNER, CHARLES M · 2007 to 2010
$1.3M
NCI NIH HHS P30 CA023108NCI NIH HHS T32 CA009658NCI NIH HHS T32-CA09658NCRR NIH HHS P20 RR018787NIGMS NIH HHS R01 GM081665PHS HHS P20-018787PHS HHS R01-081665
6 · The paper itself

Abstract

Checkpoint with forkhead-associated and RING (Chfr) is a ubiquitin ligase (E3) that establishes an antephase or prometaphase checkpoint in response to mitotic stress. Though ubiquitination is essential for checkpoint function, the sites, linkages and ubiquitin conjugating enzyme (E2) specificity are controversial. Here we dissect the function of the two Chfr homologs in S. cerevisiae, Chf1 and Chf2, overexpression of which retard cell cycle at both G(1) and G(2). Using a genetic assay, we establish that Ubc4 is required for Chf2-dependent G(1) cell cycle delay and Chf protein turnover. In contrast, Ubc13/Mms2 is required for G(2) delay and does not contribute to Chf protein turnover. By reconstituting cis and trans-ubiquitination activities of Chf proteins in purified systems and characterizing sites modified and linkages formed by tandem mass spectrometry, we discovered that Ubc13/Mms2- dependent modifications are a distinct subset of those catalyzed by Ubc4. Mutagenesis of Lys residues identified in vitro indicates that site-specific Ubc4-dependent Chf protein autoubiquitination is responsible for Chf protein turnover. Thus, combined genetic and biochemical analyses indicate that Chf proteins have dual E2 specificity accounting for different functions in the cell cycle.

Indexed as

Amino Acid SequenceBasic Helix-Loop-Helix ProteinsCell CycleCell Cycle ProteinsCell DivisionG1 PhaseG2 PhaseNeoplasm ProteinsPoly-ADP-Ribose Binding ProteinsRepressor ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsStructural Homology, ProteinUbiquitinationUbiquitin-Conjugating EnzymesUbiquitin-Protein LigasesBasic Helix-Loop-Helix ProteinsCell Cycle ProteinsCHFR protein, humanDma1 protein, S cerevisiaeHairy, HRT1 proteinMMS2 protein, S cerevisiaeNeoplasm ProteinsPoly-ADP-Ribose Binding ProteinsRepressor ProteinsSaccharomyces cerevisiae ProteinsUBC13 protein, S cerevisiaeUbc4 protein, S cerevisiaeUbiquitin-Conjugating EnzymesUbiquitin-Protein Ligases

Identifiers

PMID18202552
PMCPMC2292246
OpenAlexW2144579449

What OpenQuestion holds

Textmetadata
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.