Evidence map›Paper›PMID 26276391›Full record

ArticleThe Journal of biological chemistry2015

Prolyl isomerase Pin1 negatively regulates AMP-activated protein kinase (AMPK) by associating with the CBS domain in the γ subunit.

Yusuke Nakatsu, Misaki Iwashita, Hideyuki Sakoda, Hiraku Ono, Kengo Nagata, Yasuka Matsunaga, Toshiaki Fukushima, Midori Fujishiro, Akifumi Kushiyama, Hideaki Kamata and 6 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

22 citing papers in PubMed, 38 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Beneficial Effects of PIN1 Inhibition on Diabetes Mellitus: A Concise Review.Endocrine, metabolic & immune disorders drug targets · 2025
    Review
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Review
  13. Review
  14. Article
  15. Article
  16. Article
  17. Review
  18. Review
  19. Article
  20. 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

16 authors at 5 institutions in 1 country.

Yusuke NakatsuFrom the Department of Medical Science, Graduate School of Medicine.
Misaki Iwashitathe Department of Dental Science for Health Promotion, Graduate School of Biomedical Science, and.
Hideyuki Sakodathe Department of Internal Medicine, Graduate School of Medicine, University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-0033, Japan.
Hiraku Onothe Department of Endocrinology and Diabetes, School of Medicine, Saitama Medical University, Moroyama, Saitama 350-0495, Japan.
Kengo NagataFrom the Department of Medical Science, Graduate School of Medicine.
Yasuka MatsunagaFrom the Department of Medical Science, Graduate School of Medicine.
Toshiaki FukushimaFrom the Department of Medical Science, Graduate School of Medicine.
Midori Fujishirothe Department of Internal Medicine, Graduate School of Medicine, University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-0033, Japan.
Akifumi Kushiyamathe Division of Diabetes and Metabolism, Institute for Adult Disease, Asahi Life Foundation, 1-6-1 Marunouchi, Chiyoda-ku, Tokyo 103-0002, Japan.
Hideaki KamataFrom the Department of Medical Science, Graduate School of Medicine.
Shin-Ichiro Takahashithe Department of Applied Biological Chemistry, Graduate School of Agricultural and Life Sciences, University of Tokyo, Bunkyo-ku, Tokyo 113-8657, Japan.
Hideki Katagirithe Division of Molecular Metabolism and Diabetes, Tohoku University Graduate School of Medicine, 2-1 Seiryo-machi, Aoba-ku, Sendai 980-8574, Japan.
Hiroaki Hondathe Department of Disease Model, Research Institute of Radiation Biology and Medicine, Hiroshima University, 1-2-3 Kasumi, Minami-ku, Hiroshima City 734-8553, Hiroshima, Japan.
Hiroshi Kiyonarithe Animal Resource Development Unit and Genetic Engineering Team, Division of Bio-function Dynamics Imaging, RIKEN Center for Life Science Technologies, 2-2-3 Minatojima Minami-machi, Chuou-ku, Kobe 650-0047, Japan, and.
Takafumi Uchidathe Department of Molecular Cell Biology, Graduate School of Agricultural Science, Tohoku University Sendai, Miyagi 981-8555, Japan.
Tomoichiro AsanoFrom the Department of Medical Science, Graduate School of Medicine, tasano@hiroshima-u.ac.jp.
Hiroshima University · JPThe University of Tokyo · JPTohoku University · JPInstitute for Adult Diseases Asahi Life Foundation · JPSaitama Medical University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

AMP-activated protein kinase (AMPK) plays a critical role in metabolic regulation. In this study, first, it was revealed that Pin1 associates with any isoform of γ, but not with either the α or the β subunit, of AMPK. The association between Pin1 and the AMPK γ1 subunit is mediated by the WW domain of Pin1 and the Thr(211)-Pro-containing motif located in the CBS domain of the γ1 subunit. Importantly, overexpression of Pin1 suppressed AMPK phosphorylation in response to either 2-deoxyglucose or biguanide stimulation, whereas Pin1 knockdown by siRNAs or treatment with Pin1 inhibitors enhanced it. The experiments using recombinant Pin1, AMPK, LKB1, and PP2C proteins revealed that the protective effect of AMP against PP2C-induced AMPKα subunit dephosphorylation was markedly suppressed by the addition of Pin1. In good agreement with the in vitro data, the level of AMPK phosphorylation as well as the expressions of mitochondria-related genes, such as PGC-1α, which are known to be positively regulated by AMPK, were markedly higher with reduced triglyceride accumulation in the muscles of Pin1 KO mice as compared with controls. These findings suggest that Pin1 plays an important role in the pathogenic mechanisms underlying impaired glucose and lipid metabolism, functioning as a negative regulator of AMPK.

Indexed as

AMP-Activated Protein KinasesAnimalsGene Expression RegulationGene Expression Regulation, EnzymologicGene SilencingGlucoseHEK293 CellsHep G2 CellsHumansLipid MetabolismMetabolic SyndromeMetforminMiceMice, Inbred C57BLMice, KnockoutMice, TransgenicAMP-Activated Protein KinasesGlucoseMetforminNIMA-Interacting Peptidylprolyl IsomerasePeptidylprolyl IsomerasePIN1 protein, humanPin1 protein, mousePRKAG1 protein, humanProtein Phosphatase 2Recombinant ProteinsRNA, Small InterferingAMP-activated kinase (AMPK)diabetesenergy metabolismlipid metabolismmetabolic syndromemuscleprolyl isomerase

Identifiers

PMID26276391
PMCPMC4591812
OpenAlexW2269120582

What OpenQuestion holds

Texttitle and abstract
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.