Evidence map›Paper›PMID 25691662›Full record

ArticleMolecular and cellular biology2015

Casein kinase 1γ ensures monopolar growth polarity under incomplete DNA replication downstream of Cds1 and calcineurin in fission yeast.

Takayuki Koyano, Manabu Konishi, Sophie G Martin, Yoshikazu Ohya, Dai Hirata, Takashi Toda, Kazunori Kume

Open access · bronzeAbstract read
In one paragraph

Article in Molecular and cellular biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.5field-weighted citation impact, top 34% 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

5 citing papers in PubMed, 9 citations in OpenAlex.

  1. Review
  2. Article
  3. The Fission Yeast Mating-Type Switching Motto: "One-for-Two" and "Two-for-One".Microbiology and molecular biology reviews : MMBR · 2023
    Review
  4. Article
  5. Article
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 4 institutions in 3 countries.

Takayuki KoyanoDepartment of Molecular Biotechnology, Graduate School of Advanced Sciences of Matter, Hiroshima University, Higashi-Hiroshima, Japan Laboratory of Cell Regulation, Cancer Research UK, London Research Institute, London, United Kingdom.
Manabu KonishiDepartment of Molecular Biotechnology, Graduate School of Advanced Sciences of Matter, Hiroshima University, Higashi-Hiroshima, Japan.
Sophie G MartinUniversity of Lausanne, Department of Fundamental Microbiology, Lausanne, Switzerland.
Yoshikazu OhyaDepartment of Integrated Biosciences, Graduate School of Frontier Sciences, University of Tokyo, Kashiwa, Chiba, Japan.
Dai HirataDepartment of Molecular Biotechnology, Graduate School of Advanced Sciences of Matter, Hiroshima University, Higashi-Hiroshima, Japan.
Takashi TodaLaboratory of Cell Regulation, Cancer Research UK, London Research Institute, London, United Kingdom takashi.toda@cancer.org.uk kume513@hiroshima-u.ac.jp.
Kazunori KumeDepartment of Molecular Biotechnology, Graduate School of Advanced Sciences of Matter, Hiroshima University, Higashi-Hiroshima, Japan takashi.toda@cancer.org.uk kume513@hiroshima-u.ac.jp.
Hiroshima University · JPCancer Research UK · GBThe University of Tokyo · JPUniversity of Lausanne · CH

Funding

Cancer Research UK
6 · The paper itself

Abstract

Cell polarity is essential for various cellular functions during both proliferative and developmental stages, and it displays dynamic alterations in response to intracellular and extracellular cues. However, the molecular mechanisms underlying spatiotemporal control of polarity transition are poorly understood. Here, we show that fission yeast Cki3 (a casein kinase 1γ homolog) is a critical regulator to ensure persistent monopolar growth during S phase. Unlike the wild type, cki3 mutant cells undergo bipolar growth when S phase is blocked, a condition known to delay transition from monopolar to bipolar growth (termed NETO [new end takeoff]). Consistent with this role, Cki3 kinase activity is substantially increased, and cells lose their viability in the absence of Cki3 upon an S-phase block. Cki3 acts downstream of the checkpoint kinase Cds1/Chk2 and calcineurin, and the latter physically interacts with Cki3. Autophosphorylation in the C terminus is inhibitory toward Cki3 kinase activity, and calcineurin is responsible for its dephosphorylation. Cki3 localizes to the plasma membrane, and this localization requires the palmitoyltransferase complex Erf2-Erf4. Membrane localization is needed not only for proper NETO timing but also for Cki3 kinase activity. We propose that Cki3 acts as a critical inhibitor of cell polarity transition under S-phase arrest.

Indexed as

DNA ReplicationAmino Acid SequenceCalcineurinCasein Kinase ICheckpoint Kinase 2Gene DeletionMolecular Sequence DataPhosphorylationSchizosaccharomycesSchizosaccharomyces pombe ProteinsCalcineurinCasein Kinase ICds1 protein, S pombeCheckpoint Kinase 2Cki3 protein, S pombeSchizosaccharomyces pombe Proteins

Identifiers

PMID25691662
PMCPMC4387218
OpenAlexW2019022658

What OpenQuestion holds

Textmetadata
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.