Evidence map›Paper›PMID 22266860›Full record

ArticleOncogene2012

Sp1 phosphorylation by cyclin-dependent kinase 1/cyclin B1 represses its DNA-binding activity during mitosis in cancer cells.

J-Y Chuang, S-A Wang, W-B Yang, H-C Yang, C-Y Hung, T-P Su, W-C Chang, J-J Hung

Open access · bronzeAbstract read
In one paragraph

Article in Oncogene, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
1.6field-weighted citation impact, top 18% 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

32 citing papers in PubMed, 50 citations in OpenAlex.

  1. Unraveling the role of specificity protein 1 in gliomas: pathophysiology and clinical implications.Clinical & translational oncology : official publication of the Federation of Spanish Oncology Societies and of the National Cancer Institute of Mexico · 2026
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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

8 authors at 3 institutions in 2 countries.

J-Y ChuangInstitute of Bioinformatics and Biosignal Transduction, College of Bioscience and Biotechnology, Tainan, Taiwan.
S-A Wang
W-B Yang
H-C Yang
C-Y Hung
T-P Su
W-C Chang
J-J Hung
National Tainan Institute of Nursing · TWNational Cheng Kung University · TWNational Institute on Drug Abuse · US

Funding

Biological And Biochemical Characterization Of Sigma ReceptorsZIADA000206 · NIDA · NATIONAL INSTITUTE ON DRUG ABUSE · PI SU, TSUNG PING · 2009 to 2025
$23.6M
Intramural NIH HHS Z99 DA999999
6 · The paper itself

Abstract

Sp1 is important for the transcription of many genes. Our previous studies have shown that Sp1 is degraded in normal cell, but it is preserved in cancer cells during mitosis and exists a priori in the daughter cells, ready to engage in gene transcription and thereby contributes to the proliferation and survival of cancer cells. The mechanism by which Sp1 is preserved in cancer cells during mitosis remains unknown. In this study, we observed that Sp1 strongly colocalized with cyclin-dependent kinase 1 (CDK1)/cyclin B1 during mitosis. Moreover, we showed that Sp1 is a novel mitotic substrate of CDK1/cyclin B1 and is phosphorylated by it at Thr 739 before the onset of mitosis. Phospho-Sp1 reduced its DNA-binding ability and facilitated the chromatin condensation process during mitosis. Mutation of Thr739 to alanine resulted in Sp1 remaining in the chromosomes, delayed cell-cycle progression, and eventually led to apoptosis. Screening of Sp1-associated proteins during mitosis by using liquid chromatography/mass spectrometry indicated the tethering of Sp1 to myosin/F-actin. Furthermore, phospho-Sp1 and myosin/F-actin appeared to exist as a congregated ring at the periphery of the chromosome. However, at the end of mitosis and the beginning of interphase, Sp1 was dephosphorylated by PP2A and returned to the chromatin. These results indicate that cancer cells use CDK1 and PP2A to regulate the movement of Sp1 in and out of the chromosomes during cell-cycle progression, which may benefit cancer-cell proliferation.

Indexed as

Gene Expression Regulation, NeoplasticMitosisActinsAdenocarcinomaAmino Acid MotifsAnimalsCDC2 Protein KinaseChromatin Assembly and DisassemblyCyclin B1Enzyme ActivationFemaleHeLa CellsHumansInterphaseMammary Neoplasms, AnimalMethylnitrosoureaActinsCCNB1 protein, humanCDC2 Protein KinaseCyclin B1MethylnitrosoureaMyosinsProtein Phosphatase 2Sp1 Transcription FactorThreonine

Identifiers

PMID22266860
PMCPMC3707305
OpenAlexW2002170815

What OpenQuestion holds

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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.