Evidence map›Paper›PMID 29166606›Full record

ArticleCell reports2017

SUMOylation Promotes Nuclear Import and Stabilization of Polo-like Kinase 1 to Support Its Mitotic Function.

Donghua Wen, Jianguo Wu, Lei Wang, Zheng Fu

Open access · goldAbstract read
In one paragraph

Article in Cell reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
2.9field-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

45 citing papers in PubMed, 71 citations in OpenAlex.

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  13. SUMO modifies GβL and mediates mTOR signaling.The Journal of biological chemistry · 2024
    Article
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  20. Sumoylation regulates functional properties of the oocyte transcription factors SOHLH1 and NOBOX.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2023
    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

4 authors at 1 institution in 1 country.

Donghua WenDepartment of Human and Molecular Genetics, Institute of Molecular Medicine, Massey Cancer Center, Virginia Commonwealth University, School of Medicine, Richmond, VA 23298, USA.
Jianguo WuDepartment of Human and Molecular Genetics, Institute of Molecular Medicine, Massey Cancer Center, Virginia Commonwealth University, School of Medicine, Richmond, VA 23298, USA.
Lei WangDepartment of Human and Molecular Genetics, Institute of Molecular Medicine, Massey Cancer Center, Virginia Commonwealth University, School of Medicine, Richmond, VA 23298, USA.
Zheng FuDepartment of Human and Molecular Genetics, Institute of Molecular Medicine, Massey Cancer Center, Virginia Commonwealth University, School of Medicine, Richmond, VA 23298, USA. Electronic address: zheng.fu@vcuhealth.org.
Virginia Commonwealth University · US

Funding

The role of PLK1 in prostate cancerR01CA191002 · NCI · VIRGINIA COMMONWEALTH UNIVERSITY · PI FU, ZHENG · 2016 to 2020
$1.7M
NCI NIH HHS R01 CA191002
6 · The paper itself

Abstract

As a pivotal mitotic regulator, polo-like kinase 1 (PLK1) is under highly coordinated and multi-layered regulation. However, the pathways that control PLK1's activity and function have just begun to be elucidated. PLK1 has recently been shown to be functionally modulated by post-translational modifications (PTMs), including phosphorylation and ubiquitination. Herein, we report that SUMOylation plays an essential role in regulating PLK1's mitotic function. We found that Ubc9 was recruited to PLK1 upon initial phosphorylation and activation by CDK1/cyclin B. By in vivo and in vitro SUMOylation assays, PLK1 was identified as a physiologically relevant small ubiquitin-related modifier (SUMO)-targeted protein, preferentially modified by SUMO-1. We further showed that K492 on PLK1 is essential for SUMOylation. SUMOylation causes PLK1's nuclear import and significantly increases its protein stability, both of which are critical for normal mitotic progression and genomic integrity. Our findings suggest that SUMOylation is an important regulatory mechanism governing PLK1's mitotic function.

Indexed as

Active Transport, Cell NucleusCDC2 Protein KinaseCell Cycle ProteinsCyclin BHumansMitosisPhosphorylationPolo-Like Kinase 1Protein Processing, Post-TranslationalProtein Serine-Threonine KinasesProto-Oncogene ProteinsSmall Ubiquitin-Related Modifier ProteinsSUMO-1 ProteinSumoylationCDC2 Protein KinaseCell Cycle ProteinsCyclin BPolo-Like Kinase 1Protein Serine-Threonine KinasesProto-Oncogene ProteinsSmall Ubiquitin-Related Modifier ProteinsSUMO-1 Proteingenomic stabilitymitotic progressionnuclear importPLK1protein stabilitySUMOylationUbc9

Identifiers

PMID29166606
PMCPMC5728694
OpenAlexW2770515616

What OpenQuestion holds

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Registered trials

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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.