Evidence map›Paper›PMID 23217712›Full record

ArticleCell2012

CDK-dependent Hsp70 Phosphorylation controls G1 cyclin abundance and cell-cycle progression.

Andrew W Truman, Kolbrun Kristjansdottir, Donald Wolfgeher, Naushaba Hasin, Sigrun Polier, Hong Zhang, Sarah Perrett, Chrisostomos Prodromou, Gary W Jones, Stephen J Kron

Open access · hybridAbstract read
In one paragraph

Article in Cell, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 94 papers.

0numbers the graph read from it
0cells of the map it votes in
94citing papers in PubMed
3.5field-weighted citation impact, top 6% 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

94 citing papers in PubMed, 146 citations in OpenAlex.

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34 more citing papers are in PubMed but not listed here.

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

10 authors at 4 institutions in 4 countries.

Andrew W TrumanLudwig Center for Metastasis Research, The University of Chicago, Chicago, IL 60637, USA.
Kolbrun Kristjansdottir
Donald Wolfgeher
Naushaba Hasin
Sigrun Polier
Hong Zhang
Sarah Perrett
Chrisostomos Prodromou
Gary W Jones
Stephen J Kron
University of Chicago · USChinese Academy of Sciences · CNNational University of Ireland, Maynooth · IEUniversity of Sussex · GB

Funding

Radiation response within the tumor microenvironmentR01CA164492 · NCI · UNIVERSITY OF CHICAGO · PI KRON, STEPHEN J. · 2011 to 2015
$4.8M
RADIATION INDUCED G1 CHECKPOINT ARREST IN YEASTR01GM060443 · NIGMS · UNIVERSITY OF CHICAGO · PI KRON, STEPHEN J. · 1999 to 2010
$1.8M
NCI NIH HHS R01 CA164492NIGMS NIH HHS GM60443NIGMS NIH HHS R01 GM060443Wellcome Trust 095605Wellcome Trust 095605/Z11/Z
6 · The paper itself

Abstract

In budding yeast, the essential functions of Hsp70 chaperones Ssa1-4 are regulated through expression level, isoform specificity, and cochaperone activity. Suggesting a novel regulatory paradigm, we find that phosphorylation of Ssa1 T36 within a cyclin-dependent kinase (CDK) consensus site conserved among Hsp70 proteins alters cochaperone and client interactions. T36 phosphorylation triggers displacement of Ydj1, allowing Ssa1 to bind the G1 cyclin Cln3 and promote its degradation. The stress CDK Pho85 phosphorylates T36 upon nitrogen starvation or pheromone stimulation, destabilizing Cln3 to delay onset of S phase. In turn, the mitotic CDK Cdk1 phosphorylates T36 to block Cln3 accumulation in G2/M. Suggesting broad conservation from yeast to human, CDK-dependent phosphorylation of Hsc70 T38 similarly regulates Cyclin D1 binding and stability. These results establish an active role for Hsp70 chaperones as signal transducers mediating growth control of G1 cyclin abundance and activity.

Indexed as

Adenosine TriphosphatasesCell CycleCell ProliferationCyclin D1CyclinsHEK293 CellsHSC70 Heat-Shock ProteinsHSP70 Heat-Shock ProteinsHumansPhosphorylationSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsAdenosine TriphosphatasesCLN3 protein, S cerevisiaeCyclin D1CyclinsHSC70 Heat-Shock ProteinsHSP70 Heat-Shock ProteinsSaccharomyces cerevisiae ProteinsSSA1 protein, S cerevisiae

Identifiers

PMID23217712
PMCPMC3778871
OpenAlexW2159893325

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.