Evidence map›Paper›PMID 18199680›Full record

ArticleMolecular biology of the cell2008

Phosphorylation by c-Jun NH2-terminal kinase 1 regulates the stability of transcription factor Sp1 during mitosis.

Jian-Ying Chuang, Yi-Ting Wang, Shiu-Hwa Yeh, Yi-Wen Liu, Wen-Chang Chang, Jan-Jong Hung

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 62 papers.

0numbers the graph read from it
0cells of the map it votes in
62citing papers in PubMed
4.3field-weighted citation impact, top 5% 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

62 citing papers in PubMed, 115 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
    Review
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  6. Role of post-translational modifications of Sp1 in cancer: state of the art.Frontiers in cell and developmental biology · 2024
    Review
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  14. Bacterial Lipoproteins Induce BAFF ProductionFrontiers in immunology · 2020
    Article
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  17. Ursolic acid facilitates apoptosis in rheumatoid arthritis synovial fibroblasts by inducing SP1-mediated Noxa expression and proteasomal degradation of Mcl-1.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2018
    Article
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2 more citing papers are in PubMed but not listed here.

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

6 authors at 3 institutions in 2 countries.

Jian-Ying ChuangInstitute of Basic Medical Sciences, College of Medicine, National Cheng-Kung University, Tainan 701, Taiwan.
Yi-Ting Wang
Shiu-Hwa Yeh
Yi-Wen Liu
Wen-Chang Chang
Jan-Jong Hung
Institute of Physiology and Basic Medicine · RUNational Cheng Kung University · TWNational Chiayi University · TW

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The transcription factor Sp1 is ubiquitously expressed in different cells and thereby regulates the expression of genes involved in many cellular processes. This study reveals that Sp1 was phosphorylated during the mitotic stage in three epithelial tumor cell lines and one glioma cell line. By using different kinase inhibitors, we found that during mitosis in HeLa cells, the c-Jun NH(2)-terminal kinase (JNK) 1 was activated that was then required for the phosphorylation of Sp1. In addition, blockade of the Sp1 phosphorylation via inhibition JNK1 activity in mitosis resulted in the ubiquitination and degradation of Sp1. JNK1 phosphorylated Sp1 at Thr278/739. The Sp1 mutated at Thr278/739 was unstable during mitosis, possessing less transcriptional activity for the 12(S)-lipoxygenase expression and exhibiting a decreased cell growth rate compared with wild-type Sp1 in HeLa cells. In N-methyl-N-nitrosourea-induced mammary tumors, JNK1 activation provided a potential relevance with the accumulation of Sp1. Together, our results indicate that JNK1 activation is necessary to phosphorylate Sp1 and to shield Sp1 from the ubiquitin-dependent degradation pathway during mitosis in tumor cell lines.

Indexed as

MitosisAnimalsArachidonate 12-LipoxygenaseCell Line, TumorCell ProliferationEnzyme ActivationFemaleHumansMethylnitrosoureaMitogen-Activated Protein Kinase 8Mutant ProteinsNeoplasmsPhosphorylationPhosphothreonineProtein TransportRatsArachidonate 12-LipoxygenaseMethylnitrosoureaMitogen-Activated Protein Kinase 8Mutant ProteinsPhosphothreonineSp1 Transcription Factor

Identifiers

PMID18199680
PMCPMC2262957
OpenAlexW2130953564

What OpenQuestion holds

Textmetadata
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.