Evidence map›Paper›PMID 33251722›Full record

ArticleEMBO reports2021

AMPK regulates cell shape of cardiomyocytes by modulating turnover of microtubules through CLIP-170.

Shohei Yashirogi, Takemasa Nagao, Yuya Nishida, Yusuke Takahashi, Tasneem Qaqorh, Issei Yazawa, Toru Katayama, Hidetaka Kioka, Tsubasa S Matsui, Shigeyoshi Saito and 9 more

Open access · greenAbstract read
In one paragraph

Article in EMBO reports, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed, 1 pooled it
1.3field-weighted citation impact, top 19% 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

16 citing papers in PubMed, 1 synthesis or guideline pooled it, 25 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Circulation. Heart failure · 2025
    Article
  4. LSMEM2, Localized at the Neuromuscular Junction, Modulates Mitochondrial Integration in Skeletal Muscles.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2025
    Article
  5. Article
  6. Ion channel trafficking implications in heart failure.Frontiers in cardiovascular medicine · 2024
    Review
  7. Review
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Review
  15. Mechanisms and Regulation of Cardiac CaInternational journal of molecular sciences · 2021
    Review
  16. Article
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

19 authors at 5 institutions in 1 country.

Shohei YashirogiDepartment of Medical Biochemistry, Osaka University Graduate School of Frontier Biological Science, Suita, Osaka, Japan.
Takemasa NagaoDepartment of Medical Biochemistry, Osaka University Graduate School of Frontier Biological Science, Suita, Osaka, Japan.
Yuya NishidaDepartment of Medical Biochemistry, Osaka University Graduate School of Frontier Biological Science, Suita, Osaka, Japan.
Yusuke TakahashiDepartment of Molecular Pharmacology, National Cerebral and Cardiovascular Center, Suita, Osaka, Japan.
Tasneem QaqorhDepartment of Medical Biochemistry, Osaka University Graduate School of Frontier Biological Science, Suita, Osaka, Japan.
Issei YazawaDepartment of Medical Biochemistry, Osaka University Graduate School of Frontier Biological Science, Suita, Osaka, Japan.
Toru KatayamaDepartment of Medical Biochemistry, Osaka University Graduate School of Frontier Biological Science, Suita, Osaka, Japan.
Hidetaka KiokaDepartment of Cardiovascular Medicine, Osaka University Graduate School of Medicine, Suita, Osaka, Japan.
Tsubasa S MatsuiDivision of Bioengineering, Graduate School of Engineering Science, Osaka University, Toyonaka, Japan.
Shigeyoshi SaitoDepartment of Biomedical Imaging, National Cardiovascular and Cerebral Research Center, Suita, Osaka, Japan.
Yuki MasumuraDepartment of Cardiovascular Medicine, Osaka University Graduate School of Medicine, Suita, Osaka, Japan.
Osamu TsukamotoDepartment of Medical Biochemistry, Osaka University Graduate School of Frontier Biological Science, Suita, Osaka, Japan.
Hisakazu KatoDepartment of Medical Biochemistry, Osaka University Graduate School of Frontier Biological Science, Suita, Osaka, Japan.
Hiromichi UedaDepartment of Cardiovascular Medicine, Osaka University Graduate School of Medicine, Suita, Osaka, Japan.
Osamu YamaguchiDepartment of Cardiovascular Medicine, Osaka University Graduate School of Medicine, Suita, Osaka, Japan.
Kenta YashiroDivision of Anatomy and Developmental Biology, Department of Anatomy, Kyoto Prefectural University of Medicine, Kyoto, Japan.
Satoru YamazakiDepartment of Molecular Pharmacology, National Cerebral and Cardiovascular Center, Suita, Osaka, Japan.
Seiji TakashimaDepartment of Medical Biochemistry, Osaka University Graduate School of Frontier Biological Science, Suita, Osaka, Japan.
Yasunori ShintaniDepartment of Medical Biochemistry, Osaka University Graduate School of Frontier Biological Science, Suita, Osaka, Japan.ORCID 0000-0001-9579-0727
National Cerebral and Cardiovascular Center · JPThe University of Osaka · JPEhime University · JPJapan Science and Technology Agency · JPKyoto Prefectural University of Medicine · JP

Funding

Medical Research Council MR/J007625/1
6 · The paper itself

Abstract

AMP-activated protein kinase (AMPK) is a multifunctional kinase that regulates microtubule (MT) dynamic instability through CLIP-170 phosphorylation; however, its physiological relevance in vivo remains to be elucidated. In this study, we identified an active form of AMPK localized at the intercalated disks in the heart, a specific cell-cell junction present between cardiomyocytes. A contractile inhibitor, MYK-461, prevented the localization of AMPK at the intercalated disks, and the effect was reversed by the removal of MYK-461, suggesting that the localization of AMPK is regulated by mechanical stress. Time-lapse imaging analysis revealed that the inhibition of CLIP-170 Ser-311 phosphorylation by AMPK leads to the accumulation of MTs at the intercalated disks. Interestingly, MYK-461 increased the individual cell area of cardiomyocytes in CLIP-170 phosphorylation-dependent manner. Moreover, heart-specific CLIP-170 S311A transgenic mice demonstrated elongation of cardiomyocytes along with accumulated MTs, leading to progressive decline in cardiac contraction. In conclusion, these findings suggest that AMPK regulates the cell shape and aspect ratio of cardiomyocytes by modulating the turnover of MTs through homeostatic phosphorylation of CLIP-170 at the intercalated disks.

Indexed as

AMP-Activated Protein KinasesMyocytes, CardiacAnimalsCell ShapeMiceMicrotubule-Associated ProteinsMicrotubulesNeoplasm ProteinsPhosphorylationAMP-Activated Protein Kinasescytoplasmic linker protein 170Microtubule-Associated ProteinsNeoplasm ProteinsAMPKCLIP-170intercalated diskmicrotubule

Identifiers

PMID33251722
PMCPMC7788454
OpenAlexW3109772286

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.