Evidence map›Paper›PMID 33280247›Full record

ArticleCytoskeleton (Hoboken, N.J.)2020

The phosphatase inhibitor Sds23 promotes symmetric spindle positioning in fission yeast.

Katherine L Schutt, James B Moseley

Open access · greenAbstract read
In one paragraph

Article in Cytoskeleton (Hoboken, N.J.), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.3field-weighted citation impact, top 44% 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

3 citing papers in PubMed, 5 citations in OpenAlex.

  1. Article
  2. Article
  3. 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

2 authors at 1 institution in 1 country.

Katherine L SchuttDepartment of Biochemistry and Cell Biology, The Geisel School of Medicine at Dartmouth, Hanover, New Hampshire, USA.
James B MoseleyDepartment of Biochemistry and Cell Biology, The Geisel School of Medicine at Dartmouth, Hanover, New Hampshire, USA.
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 MADDEN, DEAN R · 2016 to 2025
$25.9M
Molecular and Cellular Biology at DartmouthT32GM008704 · NIGMS · DARTMOUTH COLLEGE · PI COMPTON, DUANE A. · 1998 to 2018
$6.8M
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
NCI NIH HHS P30 CA023108NIGMS NIH HHS P20 GM113132NIGMS NIH HHS R01 GM099774NIGMS NIH HHS R01 GM133856NIGMS NIH HHS T32 GM008704
6 · The paper itself

Abstract

A hallmark of cell division in eukaryotic cells is the formation and elongation of a microtubule (MT)-based mitotic spindle. Proper positioning of the spindle is critical to ensure equal segregation of the genetic material to the resulting daughter cells. Both the timing of spindle elongation and constriction of the actomyosin contractile ring must be precisely coordinated to prevent missegregation or damage to the genetic material during cellular division. Here, we show that Sds23, an inhibitor of protein phosphatases, contributes to proper positioning of elongating spindles in fission yeast cells. We found that sds23∆ mutant cells exhibit asymmetric spindles that initially elongate asymmetrically toward one end of the dividing cell. Spindle asymmetry in sds23∆ cells results from a defect that is distinct from previously identified mechanisms, including MT protrusions and enlarged vacuoles. Combined with our previous work, this study demonstrates that Sds23, an inhibitor of PP2A-family protein phosphatases, promotes proper positioning of both the bipolar spindle and cytokinetic ring during fission yeast cell division. These two steps ensure the overall symmetry and fidelity of the cell division process.

Indexed as

Cell Cycle ProteinsSchizosaccharomycesSchizosaccharomyces pombe ProteinsSpindle ApparatusCell Cycle ProteinsSchizosaccharomyces pombe ProteinsSds23 protein, S pombemicrotubulesmitosisphosphatasepombeSds23spindle

Identifiers

PMID33280247
PMCPMC8195570
OpenAlexW3113295124

What OpenQuestion holds

Textmetadata
LicenceTDM
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.