Evidence map›Paper›PMID 24508166›Full record

ArticleCurrent biology : CB2014

Dueling kinases regulate cell size at division through the SAD kinase Cdr2.

Lin Deng, Suzanne Baldissard, Arminja N Kettenbach, Scott A Gerber, James B Moseley

Open access · bronzeAbstract read
In one paragraph

Article in Current biology : CB, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
2.8field-weighted citation impact, top 9% 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

26 citing papers in PubMed, 40 citations in OpenAlex.

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  14. Controlling cell size through sizer mechanisms.Current opinion in systems biology · 2017
    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

5 authors at 1 institution in 1 country.

Lin DengDepartment of Biochemistry, The Geisel School of Medicine at Dartmouth, Hanover, NH 03755, USA.
Suzanne BaldissardDepartment of Biochemistry, The Geisel School of Medicine at Dartmouth, Hanover, NH 03755, USA.
Arminja N KettenbachDepartment of Biochemistry, The Geisel School of Medicine at Dartmouth, Hanover, NH 03755, USA; Department of Genetics and Norris Cotton Cancer Center, The Geisel School of Medicine at Dartmouth, Hanover, NH 03755, USA.
Scott A GerberDepartment of Genetics and Norris Cotton Cancer Center, The Geisel School of Medicine at Dartmouth, Hanover, NH 03755, USA.
James B MoseleyDepartment of Biochemistry, The Geisel School of Medicine at Dartmouth, Hanover, NH 03755, USA. Electronic address: james.b.moseley@dartmouth.edu.
Dartmouth College · US

Funding

Translational Engineering in Cancer (TEC)P30CA023108 · NCI · DARTMOUTH COLLEGE · PI Steven D Leach · 1985 to 2026
$91.3M
Mechanisms that coordinate cell size with mitotic entryR01GM099774 · NIGMS · DARTMOUTH COLLEGE · PI MOSELEY, JAMES B · 2012 to 2023
$3.9M
Translational phosphoproteomics for lung cancerR01CA155260 · NCI · DARTMOUTH COLLEGE · PI GERBER, SCOTT A. · 2011 to 2015
$1.8M
NCI NIH HHS P30 CA023108NCI NIH HHS R01 CA155260NCI NIH HHS R01-CA155260NIGMS NIH HHS R01 GM099774NIGMS NIH HHS R01-GM099774
6 · The paper itself

Abstract

Cell size control requires mechanisms that integrate cell growth and division. Key to this integration in fission yeast is the SAD family kinase Cdr2, which organizes a set of cortical nodes in the cell middle to promote mitotic entry through Wee1 and Cdk1. Cdr2 is inhibited by a spatial gradient of the DYRK kinase Pom1 emanating from cell tips in a cell-size-dependent manner, but how the Pom1 gradient inhibits Cdr2 activity during cell growth is unknown. Here, we show that Pom1 acts to prevent activation of Cdr2 kinase activity by the CaMKK Ssp1. We found that Ssp1 activates Cdr2 through phosphorylation of a conserved threonine residue (Thr166) in the activation loop of the Cdr2 N-terminal kinase domain both in vitro and in cells. The levels of this activating phosphorylation increased with cell-cycle progression, and genetic epistasis demonstrated that Ssp1 promotes mitotic entry through Cdr2. Intriguingly, Pom1 phosophorylated the C-terminal domain of Cdr2, and this modification reduced Cdr2-T166 phosphorylation by Ssp1. These findings show how activation of the conserved mitotic inducer Cdr2 is integrated with an inhibitory spatial gradient to ensure proper cell size control at mitosis.

Indexed as

Amino Acid SequenceAnimalsCell DivisionCell SizeHSP70 Heat-Shock ProteinsHumansPhosphorylationProtein KinasesProtein Serine-Threonine KinasesSchizosaccharomycesSchizosaccharomyces pombe ProteinsSequence AlignmentSequence Homology, Amino AcidCdr2 protein, S pombeHSP70 Heat-Shock ProteinsPom1 protein, S pombeProtein KinasesProtein Serine-Threonine KinasesPSS1 protein, S pombeSchizosaccharomyces pombe Proteins

Identifiers

PMID24508166
PMCPMC4055034
OpenAlexW1994963795

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.