Evidence map›Paper›PMID 29249658›Full record

ArticleCurrent biology : CB2018

Mechanisms Connecting the Conserved Protein Kinases Ssp1, Kin1, and Pom1 in Fission Yeast Cell Polarity and Division.

Mid Eum Lee, Scott F Rusin, Nicole Jenkins, Arminja N Kettenbach, James B Moseley

Open access · bronzeAbstract read
In one paragraph

Article in Current biology : CB, 2018. 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
2.1field-weighted citation impact, top 12% 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, 39 citations in OpenAlex.

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  16. Loss of FZO1 gene results in changes of cell dynamics in fission yeast.International journal of molecular medicine · 2020
    Article
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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.

Mid Eum LeeDepartment of Biochemistry and Cell Biology, The Geisel School of Medicine at Dartmouth, Hanover, NH 03755, USA.
Scott F RusinDepartment of Biochemistry and Cell Biology, The Geisel School of Medicine at Dartmouth, Hanover, NH 03755, USA.
Nicole JenkinsDepartment of Biochemistry and Cell Biology, The Geisel School of Medicine at Dartmouth, Hanover, NH 03755, USA; Norris Cotton Cancer Center, The Geisel School of Medicine at Dartmouth, Lebanon, NH 03756, USA.
Arminja N KettenbachDepartment of Biochemistry and Cell Biology, The Geisel School of Medicine at Dartmouth, Hanover, NH 03755, USA; Norris Cotton Cancer Center, The Geisel School of Medicine at Dartmouth, Lebanon, NH 03756, USA.
James B MoseleyDepartment of Biochemistry and Cell Biology, The Geisel School of Medicine at Dartmouth, Hanover, NH 03755, USA. Electronic address: james.b.moseley@dartmouth.edu.
Dartmouth College · US

Funding

Molecular and Cellular Biology at DartmouthT32GM008704 · NIGMS · DARTMOUTH COLLEGE · PI COMPTON, DUANE A. · 1998 to 2018
$6.8M
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
NIGMS NIH HHS R01 GM099774NIGMS NIH HHS R35 GM119455NIGMS NIH HHS T32 GM008704
6 · The paper itself

Abstract

Connections between the protein kinases that function within complex cell polarity networks are poorly understood. Rod-shaped fission yeast cells grow in a highly polarized manner, and genetic screens have identified many protein kinases, including the CaMKK-like Ssp1 and the MARK/PAR-1 family kinase Kin1, that are required for polarized growth and cell shape, but their functional mechanisms and connections have been unknown [1-5]. We found that Ssp1 promotes cell polarity by phosphorylating the activation loop of Kin1. Kin1 regulates cell polarity and cytokinesis through unknown mechanisms [4-7]. We performed a large-scale phosphoproteomic screen and found that Kin1 phosphorylates itself and Pal1 to promote growth at cell tips, and these proteins are interdependent for localization to growing cell tips. Additional Kin1 substrates for cell polarity and cytokinesis (Tea4, Mod5, Cdc15, and Cyk3) were also phosphorylated by a second kinase, the DYRK family member Pom1 [8]. Kin1 and Pom1 were enriched at opposite ends of growing cells, and they phosphorylated largely non-overlapping sites on shared substrates. Combined inhibition of both Kin1and Pom1 led to synthetic defects in their shared substrates Cdc15 and Cyk3, confirming a non-redundant functional connection through shared substrates. These findings uncover a new Ssp1-Kin1 signaling pathway, and define its functional and mechanistic connection with Pom1 signaling for cell polarity and cytokinesis. These kinases are conserved in many eukaryotes including humans, suggesting that similar connections and mechanisms might operate in a broad range of cells.

Indexed as

Cell DivisionCell PolarityHSP70 Heat-Shock ProteinsPhosphorylationProtein KinasesProtein Serine-Threonine KinasesSchizosaccharomycesSchizosaccharomyces pombe ProteinsSignal TransductionHSP70 Heat-Shock Proteinskin1 protein, S pombePom1 protein, S pombeProtein KinasesProtein Serine-Threonine KinasesPSS1 protein, S pombeSchizosaccharomyces pombe ProteinscytokinesisKin1kinasepolarityPom1pombeSsp1yeast

Identifiers

PMID29249658
PMCPMC5760279
OpenAlexW2772108201

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.