Evidence map›Paper›PMID 25635515›Full record

ArticleNature communications2015

Augmented AMPK activity inhibits cell migration by phosphorylating the novel substrate Pdlim5.

Yi Yan, Osamu Tsukamoto, Atsushi Nakano, Hisakazu Kato, Hidetaka Kioka, Noriaki Ito, Shuichiro Higo, Satoru Yamazaki, Yasunori Shintani, Ken Matsuoka and 8 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2015. 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
5.2field-weighted citation impact, top 4% 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, 94 citations in OpenAlex.

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  9. The IPBiochimica et biophysica acta. Molecular basis of disease · 2025
    Article
  10. Article
  11. Exploring the PDZ, DUF, and LIM Domains of Pdlim5 in Dendrite Branching.International journal of molecular sciences · 2024
    Article
  12. LKB1 biology: assessing the therapeutic relevancy of LKB1 inhibitors.Cell communication and signaling : CCS · 2024
    Review
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  15. Review
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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

18 authors at 4 institutions in 2 countries.

Yi YanDepartment of Medical Biochemistry, Osaka University Graduate School of Medicine, 2-2 Yamadaoka, Suita, Osaka 565-0871, Japan.
Osamu TsukamotoDepartment of Medical Biochemistry, Osaka University Graduate School of Medicine, 2-2 Yamadaoka, Suita, Osaka 565-0871, Japan.
Atsushi NakanoDepertment of Clinical Research and Development, National Cerebral and Cardiovascular Center Research Institute, Suita, Osaka 565-8565, Japan.
Hisakazu KatoDepartment of Medical Biochemistry, Osaka University Graduate School of Medicine, 2-2 Yamadaoka, Suita, Osaka 565-0871, Japan.
Hidetaka KiokaDepartment of Cardiovascular Medicine, Osaka University Graduate School of Medicine, 2-2 Yamadaoka, Suita, Osaka 565-0871, Japan.
Noriaki ItoDepartment of Cardiovascular Medicine, Osaka University Graduate School of Medicine, 2-2 Yamadaoka, Suita, Osaka 565-0871, Japan.
Shuichiro HigoDepartment of Cardiovascular Medicine, Osaka University Graduate School of Medicine, 2-2 Yamadaoka, Suita, Osaka 565-0871, Japan.
Satoru YamazakiDepartment of Cell Biology, National Cerebral and Cardiovascular Center Research Institute, Suita, Osaka 565-8565, Japan.
Yasunori ShintaniDepartment of Medical Biochemistry, Osaka University Graduate School of Medicine, 2-2 Yamadaoka, Suita, Osaka 565-0871, Japan.
Ken MatsuokaDepartment of Cardiovascular Medicine, Osaka University Graduate School of Medicine, 2-2 Yamadaoka, Suita, Osaka 565-0871, Japan.
Yulin LiaoDepartment of Cardiology, Nanfang Hospital, Southern Medical University, 1838 North Guangzhou Avenue, 510515 Guangzhou, China.
Hiroshi AsanumaDepertment of Clinical Research and Development, National Cerebral and Cardiovascular Center Research Institute, Suita, Osaka 565-8565, Japan.
Masanori AsakuraDepertment of Clinical Research and Development, National Cerebral and Cardiovascular Center Research Institute, Suita, Osaka 565-8565, Japan.
Kazuaki TakafujiCenter for Research Education, Osaka University Graduate School of Medicine, 2-2 Yamadaoka, Suita, Osaka 565-0871, Japan.
Tetsuo MinaminoDepartment of Cardiovascular Medicine, Osaka University Graduate School of Medicine, 2-2 Yamadaoka, Suita, Osaka 565-0871, Japan.
Yoshihiro AsanoDepartment of Cardiovascular Medicine, Osaka University Graduate School of Medicine, 2-2 Yamadaoka, Suita, Osaka 565-0871, Japan.
Masafumi KitakazeDepertment of Clinical Research and Development, National Cerebral and Cardiovascular Center Research Institute, Suita, Osaka 565-8565, Japan.
Seiji Takashima1] Department of Medical Biochemistry, Osaka University Graduate School of Medicine, 2-2 Yamadaoka, Suita, Osaka 565-0871, Japan [2] Japan Science and Technology Agency-Core Research for Evolutional Science and Technology (CREST), Kawaguchi 332-0012, Japan.
Osaka University · JPNational Cerebral and Cardiovascular Center · JPJapan Science and Technology Agency · JPNanfang Hospital · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Augmented AMP-activated protein kinase (AMPK) activity inhibits cell migration, possibly contributing to the clinical benefits of chemical AMPK activators in preventing atherosclerosis, vascular remodelling and cancer metastasis. However, the underlying mechanisms remain largely unknown. Here we identify PDZ and LIM domain 5 (Pdlim5) as a novel AMPK substrate and show that it plays a critical role in the inhibition of cell migration. AMPK directly phosphorylates Pdlim5 at Ser177. Exogenous expression of phosphomimetic S177D-Pdlim5 inhibits cell migration and attenuates lamellipodia formation. Consistent with this observation, S177D-Pdlim5 suppresses Rac1 activity at the cell periphery and displaces the Arp2/3 complex from the leading edge. Notably, S177D-Pdlim5, but not WT-Pdlim5, attenuates the association with Rac1-specific guanine nucleotide exchange factors at the cell periphery. Taken together, our findings indicate that phosphorylation of Pdlim5 on Ser177 by AMPK mediates inhibition of cell migration by suppressing the Rac1-Arp2/3 signalling pathway.

Indexed as

Actin-Related Protein 2-3 ComplexAdaptor Proteins, Signal TransducingAMP-Activated Protein KinasesAnimalsCell LineCell MovementMiceMicrofilament ProteinsPhosphorylationrac1 GTP-Binding ProteinSignal TransductionActin-Related Protein 2-3 ComplexAdaptor Proteins, Signal TransducingAMP-Activated Protein KinasesENH protein, mouseMicrofilament Proteinsrac1 GTP-Binding Protein

Identifiers

PMID25635515
PMCPMC4317497
OpenAlexW1991085635

What OpenQuestion holds

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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.