Evidence map›Paper›PMID 32421151›Full record

ArticleThe Journal of cell biology2020

Fission yeast Pak1 phosphorylates anillin-like Mid1 for spatial control of cytokinesis.

Joseph O Magliozzi, Jack Sears, Lauren Cressey, Marielle Brady, Hannah E Opalko, Arminja N Kettenbach, James B Moseley

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
2.6field-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

23 citing papers in PubMed, 40 citations in OpenAlex.

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  15. The Role of the Cell Integrity Pathway in Septum Assembly in Yeast.Journal of fungi (Basel, Switzerland) · 2021
    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 at 1 institution in 1 country.

Joseph O MagliozziDepartment of Biochemistry and Cell Biology, The Geisel School of Medicine at Dartmouth, Hanover, NH.
Jack SearsDepartment of Biochemistry and Cell Biology, The Geisel School of Medicine at Dartmouth, Hanover, NH.
Lauren CresseyDepartment of Biochemistry and Cell Biology, The Geisel School of Medicine at Dartmouth, Hanover, NH.
Marielle BradyDepartment of Biochemistry and Cell Biology, The Geisel School of Medicine at Dartmouth, Hanover, NH.
Hannah E OpalkoDepartment of Biochemistry and Cell Biology, The Geisel School of Medicine at Dartmouth, Hanover, NH.
Arminja N KettenbachDepartment of Biochemistry and Cell Biology, The Geisel School of Medicine at Dartmouth, Hanover, NH.
James B MoseleyDepartment of Biochemistry and Cell Biology, The Geisel School of Medicine at Dartmouth, Hanover, NH.
Dartmouth College · US

Funding

Translational Engineering in Cancer (TEC)P30CA023108 · NCI · DARTMOUTH COLLEGE · PI Fred W Kolling IV · 1985 to 2026
$91.3M
Understanding the role of RNA-binding protein mutations in cancerP20GM113132 · NIGMS · DARTMOUTH COLLEGE · PI MIERKE, DALE F · 2016 to 2025
$25.9M
Phosphorylation Signaling by Phosphoprotein PhosphatasesR35GM119455 · NIGMS · DARTMOUTH COLLEGE · PI Arminja Nadine Kettenbach · 2016 to 2026
$5.1M
Mechanisms that coordinate cell size with mitotic entryR01GM099774 · NIGMS · DARTMOUTH COLLEGE · PI MOSELEY, JAMES B · 2012 to 2023
$3.9M
Regulation of cytokinesis by cell polarity signalingR01GM133856 · NIGMS · DARTMOUTH COLLEGE · PI MOSELEY, JAMES B · 2019 to 2022
$1.5M
LC-Orbitrap MS/MS System for shotgun Proteomics at DartmouthS10OD016212 · OD · DARTMOUTH COLLEGE · PI GERBER, SCOTT A. · 2013 to 2013
$600k
NCI NIH HHS P30 CA023108NIGMS NIH HHS P20 GM113132NIGMS NIH HHS R01 GM099774NIGMS NIH HHS R01 GM133856NIGMS NIH HHS R35 GM119455NIH HHS S10 OD016212
6 · The paper itself

Abstract

Protein kinases direct polarized growth by regulating the cytoskeleton in time and space and could play similar roles in cell division. We found that the Cdc42-activated polarity kinase Pak1 colocalizes with the assembling contractile actomyosin ring (CAR) and remains at the division site during septation. Mutations in pak1 led to defects in CAR assembly and genetic interactions with cytokinesis mutants. Through a phosphoproteomic screen, we identified novel Pak1 substrates that function in polarized growth and cytokinesis. For cytokinesis, we found that Pak1 regulates the localization of its substrates Mid1 and Cdc15 to the CAR. Mechanistically, Pak1 phosphorylates the Mid1 N-terminus to promote its association with cortical nodes that act as CAR precursors. Defects in Pak1-Mid1 signaling lead to misplaced and defective division planes, but these phenotypes can be rescued by synthetic tethering of Mid1 to cortical nodes. Our work defines a new signaling mechanism driven by a cell polarity kinase that promotes CAR assembly in the correct time and place.

Indexed as

CytokinesisActomyosinCell Cycle ProteinsGene Expression Regulation, FungalGTP-Binding ProteinsMutationp21-Activated KinasesPhosphorylationSchizosaccharomycesSchizosaccharomyces pombe ProteinsSignal TransductionTime FactorsActomyosinCDC15 proteinCell Cycle ProteinsGTP-Binding ProteinsMid1 protein, S pombep21-Activated KinasesSchizosaccharomyces pombe Proteinsshk1 protein, S pombe

Identifiers

PMID32421151
PMCPMC7401808
OpenAlexW3026277514

What Socratic holds

Textmetadata
LicenceCC BY-NC-SA
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 Socratic graph.