Evidence map›Paper›PMID 23314252›Full record

ArticleNature structural & molecular biology2013

Sequential primed kinases create a damage-responsive phosphodegron on Eco1.

Nicholas A Lyons, Bryan R Fonslow, Jolene K Diedrich, John R Yates, David O Morgan

Open access · greenAbstract read
In one paragraph

Article in Nature structural & molecular biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.

0numbers the graph read from it
0cells of the map it votes in
50citing papers in PubMed
3.0field-weighted citation impact, top 8% 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

50 citing papers in PubMed, 69 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

5 authors at 2 institutions in 1 country.

Nicholas A LyonsDepartment of Physiology, University of California, San Francisco, San Francisco, California, USA.
Bryan R Fonslow
Jolene K Diedrich
John R Yates
David O Morgan
Scripps Research Institute · USUniversity of California, San Francisco · US

Funding

ZDS2P REGULATES SWE1P-DEPENDENT POLARIZED CELL GROWTH IN S CEREVISIAEP41RR011823 · NCRR · UNIVERSITY OF WASHINGTON · PI DAVIS, TRACY · 1996 to 2011
$24.7M
TrainingP41GM103533 · NIGMS · UNIVERSITY OF WASHINGTON · PI MACCOSS, MICHAEL · 2012 to 2021
$20.7M
PREDOCTORAL TRAINING IN DEVELOPMENTAL BIOLOGYT32HD007470 · NICHD · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI Todd Nystul · 1994 to 2026
$7.7M
Cell Cycle Control by Cyclin-Dependent KinasesR01GM069901 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI MORGAN, DAVID OWEN · 2004 to 2015
$3.6M
NCRR NIH HHS P41 RR011823NCRR NIH HHS P41-RR011823NICHD NIH HHS T32 HD007470NIGMS NIH HHS P41 GM103533NIGMS NIH HHS P41-GM103533NIGMS NIH HHS R01 GM069901NIGMS NIH HHS R01-GM069901
6 · The paper itself

Abstract

Sister-chromatid cohesion is established during S phase when Eco1 acetylates cohesin. In budding yeast, Eco1 activity falls after S phase due to Cdk1-dependent phosphorylation, which triggers ubiquitination by SCF(Cdc4). We show here that Eco1 degradation requires the sequential actions of Cdk1 and two additional kinases, Cdc7-Dbf4 and the GSK-3 homolog Mck1. These kinases recognize motifs primed by previous phosphorylation, resulting in an ordered sequence of three phosphorylation events on Eco1. Only the latter two phosphorylation sites are spaced correctly to bind Cdc4, resulting in strict discrimination between phosphates added by Cdk1 and by Cdc7. Inhibition of Cdc7 by the DNA damage response prevents Eco1 destruction, allowing establishment of cohesion after S phase. This elaborate regulatory system, involving three independent kinases and stringent substrate selection by a ubiquitin ligase, enables robust control of cohesion establishment during normal growth and after stress.

Indexed as

ProteolysisAcetyltransferasesBlotting, WesternCDC2 Protein KinaseCell Cycle ProteinsChromatidsChromosomal Proteins, Non-HistoneCohesinsDNA DamageF-Box ProteinsFluorescence PolarizationGlycogen Synthase Kinase 3Mass SpectrometryNuclear ProteinsPhosphorylationProtein Serine-Threonine KinasesAcetyltransferasesCDC2 Protein KinaseCDC4 protein, S cerevisiaeCDC7 protein, S cerevisiaeCell Cycle ProteinsChromosomal Proteins, Non-HistoneCohesinsECO1 protein, S cerevisiaeF-Box ProteinsGlycogen Synthase Kinase 3MCK1 protein, S cerevisiaeNuclear ProteinsProtein Serine-Threonine KinasesSaccharomyces cerevisiae ProteinsUbiquitin-Protein Ligases

Identifiers

PMID23314252
PMCPMC3565030
OpenAlexW2147418543

What OpenQuestion holds

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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.