Evidence map›Paper›PMID 26057687›Full record

ArticleScientific reports2015

Regulation of NDR1 activity by PLK1 ensures proper spindle orientation in mitosis.

Maomao Yan, Lingluo Chu, Bo Qin, Zhikai Wang, Xing Liu, Changjiang Jin, Guanglan Zhang, Marta Gomez, Alexander Hergovich, Zhengjun Chen and 3 more

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.9field-weighted citation impact, top 15% 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

18 citing papers in PubMed, 27 citations in OpenAlex.

  1. Article
  2. The NDR family of kinases: essential regulators of aging.Frontiers in molecular neuroscience · 2024
    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

13 authors at 6 institutions in 3 countries.

Maomao Yan1] Anhui Key Laboratory of Cellular Dynamics &Chemical Biology and the University of Science and Technology of China, Hefei 230026, China [2] Shanghai Institute of Biochemistry and Cell Biology, Shanghai 200031, China.
Lingluo ChuAnhui Key Laboratory of Cellular Dynamics &Chemical Biology and the University of Science and Technology of China, Hefei 230026, China.
Bo Qin1] Anhui Key Laboratory of Cellular Dynamics &Chemical Biology and the University of Science and Technology of China, Hefei 230026, China [2] Molecular Imaging Center, Morehouse School of Medicine, Atlanta, GA 30310, USA.
Zhikai Wang1] Anhui Key Laboratory of Cellular Dynamics &Chemical Biology and the University of Science and Technology of China, Hefei 230026, China [2] Molecular Imaging Center, Morehouse School of Medicine, Atlanta, GA 30310, USA.
Xing Liu1] Anhui Key Laboratory of Cellular Dynamics &Chemical Biology and the University of Science and Technology of China, Hefei 230026, China [2] Molecular Imaging Center, Morehouse School of Medicine, Atlanta, GA 30310, USA.
Changjiang JinAnhui Key Laboratory of Cellular Dynamics &Chemical Biology and the University of Science and Technology of China, Hefei 230026, China.
Guanglan ZhangGuangzhou Women and Children's Medical Center, Guangzhou 510623, China.
Marta GomezUCL Cancer Institute, University College London, London WC1E 6BT, UK.
Alexander HergovichUCL Cancer Institute, University College London, London WC1E 6BT, UK.
Zhengjun ChenShanghai Institute of Biochemistry and Cell Biology, Shanghai 200031, China.
Ping HeGuangzhou Women and Children's Medical Center, Guangzhou 510623, China.
Xinjiao GaoAnhui Key Laboratory of Cellular Dynamics &Chemical Biology and the University of Science and Technology of China, Hefei 230026, China.
Xuebiao Yao1] Anhui Key Laboratory of Cellular Dynamics &Chemical Biology and the University of Science and Technology of China, Hefei 230026, China [2] Molecular Imaging Center, Morehouse School of Medicine, Atlanta, GA 30310, USA.
University of Science and Technology of China · CNUniversity College London · GBCenter for Excellence in Molecular Cell Science · CNGuangzhou Medical University · CNGuangzhou Women and Children Medical Center · CNImaging Center · US

Funding

Morehouse School of Medicine Center of Excellence Research Endowment ProgramS21MD000101 · NIMHD · MOREHOUSE SCHOOL OF MEDICINE · PI MONTGOMERY-RICE, VALERIE C. · 2001 to 2015
$74.3M
The function of ezrin in stimulus-coupled acid secretionR01DK056292 · NIDDK · UNIVERSITY OF WISCONSIN MADISON · PI YAO, XUEBIAO · 1999 to 2012
$2.5M
Function of ACAP4 in CCL18-stimulated breast cancer metastasisR01CA164133 · NCI · MOREHOUSE SCHOOL OF MEDICINE · PI YAO, XUEBIAO · 2012 to 2016
$1.4M
Biotechnology and Biological Sciences Research Council BB/I021248/1NCI NIH HHS CA164133NCI NIH HHS R01 CA164133NIDDK NIH HHS R01 DK056292NIMHD NIH HHS S21 MD000101Wellcome TrustWellcome Trust 090090/Z/09/Z
6 · The paper itself

Abstract

Accurate chromosome segregation during mitosis requires the physical separation of sister chromatids which depends on correct position of mitotic spindle relative to membrane cortex. Although recent work has identified the role of PLK1 in spindle orientation, the mechanisms underlying PLK1 signaling in spindle positioning and orientation have not been fully illustrated. Here, we identified a conserved signaling axis in which NDR1 kinase activity is regulated by PLK1 in mitosis. PLK1 phosphorylates NDR1 at three putative threonine residues (T7, T183 and T407) at mitotic entry, which elicits PLK1-dependent suppression of NDR1 activity and ensures correct spindle orientation in mitosis. Importantly, persistent expression of non-phosphorylatable NDR1 mutant perturbs spindle orientation. Mechanistically, PLK1-mediated phosphorylation protects the binding of Mob1 to NDR1 and subsequent NDR1 activation. These findings define a conserved signaling axis that integrates dynamic kinetochore-microtubule interaction and spindle orientation control to genomic stability maintenance.

Indexed as

MitosisSpindle ApparatusCell Cycle ProteinsCell LineHumansPolo-Like Kinase 1Protein Serine-Threonine KinasesProto-Oncogene ProteinsCell Cycle ProteinsPolo-Like Kinase 1Protein Serine-Threonine KinasesProto-Oncogene ProteinsSTK38 protein, human

Identifiers

PMID26057687
PMCPMC4460818
OpenAlexW2257940210

What OpenQuestion holds

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LicenceCC BY
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.