Evidence map›Paper›PMID 28322254›Full record

ArticleScientific reports2017

Stk38 Modulates Rbm24 Protein Stability to Regulate Sarcomere Assembly in Cardiomyocytes.

Jing Liu, Xu Kong, Yew Mun Lee, Meng Kai Zhang, Li Yan Guo, Yu Lin, Teck Kwang Lim, Qingsong Lin, Xiu Qin Xu

Erratum issuedOpen 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. An erratum has been issued. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.2field-weighted citation impact, top 22% 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

20 citing papers in PubMed, 29 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. RBM24 controls cardiac QT interval through CaMKIIδ splicing.Cellular and molecular life sciences : CMLS · 2022
    Article
  7. Sarcomere maturation: function acquisition, molecular mechanism, and interplay with other organelles.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2022
    Review
  8. Review
  9. RBM20, a Therapeutic Target to Alleviate Myocardial StiffnessFrontiers in cardiovascular medicine · 2022
    Review
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. More than a messenger: Alternative splicing as a therapeutic target.Biochimica et biophysica acta. Gene regulatory mechanisms
    Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

9 authors at 2 institutions in 2 countries.

Jing LiuThe Institute of Stem Cell and Regenerative Medicine, Medical College, Xiamen University, 361100, P.R. China.
Xu KongThe Institute of Stem Cell and Regenerative Medicine, Medical College, Xiamen University, 361100, P.R. China.
Yew Mun LeeDepartment of Biological Sciences, National University of Singapore, 117543, Singapore.
Meng Kai ZhangThe Institute of Stem Cell and Regenerative Medicine, Medical College, Xiamen University, 361100, P.R. China.
Li Yan GuoThe Institute of Stem Cell and Regenerative Medicine, Medical College, Xiamen University, 361100, P.R. China.
Yu LinThe Institute of Stem Cell and Regenerative Medicine, Medical College, Xiamen University, 361100, P.R. China.
Teck Kwang LimDepartment of Biological Sciences, National University of Singapore, 117543, Singapore.
Qingsong LinDepartment of Biological Sciences, National University of Singapore, 117543, Singapore.
Xiu Qin XuThe Institute of Stem Cell and Regenerative Medicine, Medical College, Xiamen University, 361100, P.R. China.
Xiamen University · CNNational University of Singapore · SG

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

RNA-binding protein Rbm24 is a key regulator of heart development and required for sarcomere assembly and heart contractility. Yet, its underlying mechanism remains unclear. Here, we link serine/threonine kinase 38 (Stk38) signaling to the regulation of Rbm24 by showing that Rbm24 phosphorylation and its function could be modulated by Stk38. Using co-immunoprecipitation coupled with mass spectrometry technique, we identified Stk38 as an endogenous binding partner of Rbm24. Stk38 knockdown resulted in decreased Rbm24 protein level in cardiomyocytes. Further studies using Stk38 kinase inhibitor or activator showed that Rbm24 protein stability was regulated in a kinase activity-dependent manner. Deficiency of Stk38 caused reduction of sarcomere proteins and disarrangement of sarcomere, suggesting that Stk38 is essential for Rbm24 to regulate sarcomere assembly. Our results revealed that Stk38 kinase catalyzes the phosphorylation of Rbm24 during sarcomerogensis and this orchestrates accurate sarcomere alignment. This furthers our understanding of the regulatory mechanism of cardiac sarcomere assembly in both physiologic and pathologic contexts, and uncovers a potential novel pathway to cardiomyopathy through modulating the Stk38/Rbm24 protein activity.

Indexed as

Protein Processing, Post-TranslationalAnimalsCell Cycle ProteinsCell LineImmunoprecipitationIntracellular Signaling Peptides and ProteinsMass SpectrometryMice, Inbred C57BLMyocytes, CardiacN-myc Downstream-Regulated Gene 1 ProteinPhosphorylationProtein StabilityRNA-Binding ProteinsSarcomeresCell Cycle ProteinsIntracellular Signaling Peptides and ProteinsN-myc Downstream-Regulated Gene 1 ProteinRbm24 protein, mouseRNA-Binding Proteins

Identifiers

PMID28322254
PMCPMC5359592
OpenAlexW2601850833

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.