Evidence map›Paper›PMID 27169898›Full record

ArticleScientific reports2016

ALPK1 phosphorylates myosin IIA modulating TNF-α trafficking in gout flares.

Chi-Pin Lee, Shang-Lun Chiang, Albert Min-Shan Ko, Yu-Fan Liu, Che Ma, Chi-Yu Lu, Chung-Ming Huang, Jan-Gowth Chang, Tzer-Min Kuo, Chia-Lin Chen and 2 more

Erratum issuedOpen access · goldAbstract read
In one paragraph

Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
2.7field-weighted citation impact, top 11% 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

15 citing papers in PubMed, 25 citations in OpenAlex.

  1. Trial
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  7. Gain-of-function mutations inAnnals of the rheumatic diseases · 2022
    Article
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  9. Article
  10. ADP-heptose: a bacterial PAMP detected by the host sensor ALPK1.Cellular and molecular life sciences : CMLS · 2021
    Review
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

12 authors at 6 institutions in 2 countries.

Chi-Pin LeeGraduate Institute of Medicine, College of Medicine, Kaohsiung Medical University, Kaohsiung, Taiwan.
Shang-Lun ChiangEnvironment-Omics-Diseases Research Center, China Medical University Hospital, Taichung, Taiwan.
Albert Min-Shan KoDepartment of Evolutionary Genetics, Max Planck Institute for Evolutionary Anthropology, Leipzig D-04103, Germany.
Yu-Fan LiuDepartment of Biomedical Sciences, College of Medicine Sciences and Technology, Chung Shan Medical University, Taichung, Taiwan.
Che MaGenomics Research Center, Academia Sinica, Taipei, Taiwan.
Chi-Yu LuDepartment of Biochemistry, College of Medicine, Kaohsiung Medical University, Kaohsiung, Taiwan.
Chung-Ming HuangGraduate Institute of Integrated Medicines, China Medical University, Taichung, Taiwan.
Jan-Gowth ChangEpigenome Research Center, China Medical University Hospital, Taichung, Taiwan.
Tzer-Min KuoEnvironment-Omics-Diseases Research Center, China Medical University Hospital, Taichung, Taiwan.
Chia-Lin ChenDepartment of Biomedical Sciences, College of Medicine Sciences and Technology, Chung Shan Medical University, Taichung, Taiwan.
Eing-Mei TsaiGraduate Institute of Medicine, College of Medicine, Kaohsiung Medical University, Kaohsiung, Taiwan.
Ying-Chin KoEnvironment-Omics-Diseases Research Center, China Medical University Hospital, Taichung, Taiwan.
China Medical University · TWKaohsiung Medical University · TWChina Medical University Hospital · TWChung Shan Medical University · TWGenomics Research Center, Academia Sinica · TWMax Planck Institute for Evolutionary Anthropology · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Gout is characterized by the monosodium urate monohydrate (MSU)-induced arthritis. Alpha kinase-1 (ALPK1) has shown to be associated with MSU-induced inflammation and gout. Here, we used bioinformatics, proteomics, cell models, and twenty in vitro human assays to clarify some of its role in the inflammatory response to MSU. We found myosin IIA to be a frequent interacting protein partner of ALPK1, binding to its N-terminal and forming a protein complex with calmodulin and F-actin, and that MSU-induced ALPK1 phosphorylated the myosin IIA. A knockdown of endogenous ALPK1 or myosin IIA significantly reduced the MSU-induced secretion of tumour necrosis factor (TNF)-α. Furthermore, all gouty patients expressed higher basal protein levels of ALPK1, myosin IIA, and plasma TNF-α, however those medicated with colchicine has shown reduced myosin IIA and TNF-α but not ALPK1. The findings suggest ALPK1 is a kinase that participates in the regulation of Golgi-derived TNF-α trafficking through myosin IIA phosphorylation in the inflammation of gout. This novel pathway could be blocked at the level of myosin by colchicine in gout treatment.

Indexed as

Amino Acid SequenceCell LineColchicineCytokinesDown-RegulationGene Knockdown TechniquesGenetic VectorsGoutHEK293 CellsHumansModels, BiologicalMonocytesNonmuscle Myosin Type IIAPhosphorylationProtein BindingProtein DomainsColchicineCytokinesNonmuscle Myosin Type IIAProtein KinasesTumor Necrosis Factor-alphaUric Acid

Identifiers

PMID27169898
PMCPMC4864424
OpenAlexW2374914800

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.