Evidence map›Paper›PMID 29138491›Full record

ArticleScientific reports2017

SUMOylation regulates the localization and activity of Polo-like kinase 1 during cell cycle in the silkworm, Bombyx mori.

Zhiqing Li, Qixin Cui, Jian Xu, Daojun Cheng, Xiaoyan Wang, Bingqian Li, Jae Man Lee, Qingyou Xia, Takahiro Kusakabe, Ping Zhao

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
0.8field-weighted citation impact, top 30% 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

6 citing papers in PubMed, 12 citations in OpenAlex.

  1. UFMylation Modulates OFIP Stability and Centrosomal Localization.Journal of clinical laboratory analysis · 2025
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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

10 authors at 3 institutions in 2 countries.

Zhiqing LiState Key Laboratory of Silkworm Genome Biology, Southwest University, Chongqing, China.
Qixin CuiState Key Laboratory of Silkworm Genome Biology, Southwest University, Chongqing, China.
Jian XuLaboratory of Insect Genome Science, Kyushu University Graduate School of Bioresource and Bioenvironmental Sciences, Fukuoka, Japan.
Daojun ChengState Key Laboratory of Silkworm Genome Biology, Southwest University, Chongqing, China.
Xiaoyan WangState Key Laboratory of Silkworm Genome Biology, Southwest University, Chongqing, China.
Bingqian LiState Key Laboratory of Silkworm Genome Biology, Southwest University, Chongqing, China.
Jae Man LeeLaboratory of Insect Genome Science, Kyushu University Graduate School of Bioresource and Bioenvironmental Sciences, Fukuoka, Japan.
Qingyou XiaState Key Laboratory of Silkworm Genome Biology, Southwest University, Chongqing, China.
Takahiro KusakabeLaboratory of Insect Genome Science, Kyushu University Graduate School of Bioresource and Bioenvironmental Sciences, Fukuoka, Japan. kusakabe@agr.kyushu-u.ac.jp.
Ping ZhaoState Key Laboratory of Silkworm Genome Biology, Southwest University, Chongqing, China. zhaop@swu.edu.cn.
Kyushu University · JPSouthwest University · CNState Key Laboratory of Silkworm Genomic Biology

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Polo-like kinase 1 (Plk1) is a crucial cell cycle regulator by its specific localization and activity during cell cycle. It has been shown that the phosphorylation and ubiquitylation of Plk1 are required for its own activation and localization. Here, we report that SUMOylation regulates the activity of Plk1 in the lepidopteran insect of Bombyx mori. In the absence of SUMOylation, it causes the lost localization of Plk1 on centrosomes and kinetochores, as well as an uneven distribution in midzone. We further identify that the putative SUMOylation site of Bombyx Plk1 at lysine 466 is required for its localization on centrosomes, and K466 mutation in Plk1 could influence its interaction with Smt3/Ubc9 complex. These findings are also confirmed by Drosophila Polo and human Plk1, which together reveals a conserved role of Plk1 SUMOylation in mammals. Moreover, conjugation of Smt3 to Plk1 SUMOylation mutant promotes its localization on centrosomes and kinetochores, and rescues functional defects of chromosome alignment in cells depleted of endogenous Plk1. Altogether, the present data indicate that the SUMOylation of Plk1 could participate in proper chromosome alignment and segregation during mitosis, and provides a novel layer for the regulation of Plk1 localization and activity throughout cell cycle.

Indexed as

Cell CycleSumoylationAnimalsBombyxCell Cycle ProteinsCentrosomeChromosome SegregationDrosophilaInsect ProteinsKinetochoresMitosisMutationPolo-Like Kinase 1Protein Serine-Threonine KinasesProto-Oncogene ProteinsSmall Ubiquitin-Related Modifier ProteinsCell Cycle ProteinsInsect ProteinsPolo-Like Kinase 1Protein Serine-Threonine KinasesProto-Oncogene ProteinsSmall Ubiquitin-Related Modifier ProteinsUbiquitin-Conjugating Enzymes

Identifiers

PMID29138491
PMCPMC5686133
OpenAlexW2767686517

What OpenQuestion holds

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LicenceCC BY
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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.