Evidence map›Paper›PMID 20495555›Full record

ArticleNature cell biology2010

AMPK controls the speed of microtubule polymerization and directional cell migration through CLIP-170 phosphorylation.

Atsushi Nakano, Hisakazu Kato, Takashi Watanabe, Kyung-Duk Min, Satoru Yamazaki, Yoshihiro Asano, Osamu Seguchi, Shuichiro Higo, Yasunori Shintani, Hiroshi Asanuma and 6 more

Abstract read
PubMed Publisher
In one paragraph

Article in Nature cell biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 110 papers.

0numbers the graph read from it
0cells of the map it votes in
110citing papers in PubMed
7.0field-weighted citation impact, top 2% 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

110 citing papers in PubMed, 189 citations in OpenAlex.

  1. Trial
  2. 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
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Insights Into Bone Marrow Niche Stability: An Adhesion and Metabolism Route.Frontiers in cell and developmental biology · 2021
    Review

50 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

16 authors at 3 institutions in 1 country.

Atsushi NakanoDivision of Cardiovascular Medicine, National Cardiovascular Center Research Institute Suita, Osaka 565-8565, Japan.
Hisakazu Kato
Takashi Watanabe
Kyung-Duk Min
Satoru Yamazaki
Yoshihiro Asano
Osamu Seguchi
Shuichiro Higo
Yasunori Shintani
Hiroshi Asanuma
Masanori Asakura
Tetsuo Minamino
Kozo Kaibuchi
Naoki Mochizuki
Masafumi Kitakaze
Seiji Takashima
National Cerebral and Cardiovascular Center · JPOsaka University · JPNagoya University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

AMP-activated protein kinase (AMPK) is an energy-sensing Ser/Thr protein kinase originally shown to be regulated by AMP. AMPK is activated by various cellular stresses that inhibit ATP production or stimulate ATP consumption. In addition to its role in metabolism, AMPK has recently been reported to reshape cells by regulating cell polarity and division. However, the downstream targets of AMPK that participate in these functions have not been fully identified. Here, we show that phosphorylation of the microtubule plus end protein CLIP-170 by AMPK is required for microtubule dynamics and the regulation of directional cell migration. Both inhibition of AMPK and expression of a non-phosphorylatable CLIP-170 mutant resulted in prolonged and enhanced accumulation of CLIP-170 at microtubule tips, and slower tubulin polymerization. Furthermore, inhibition of AMPK impaired microtubule stabilization and perturbed directional cell migration. All of these phenotypes were rescued by expression of a phosphomimetic CLIP-170 mutant. Our results demonstrate, therefore, that AMPK controls basic cellular functions by regulating microtubule dynamics through CLIP-170 phosphorylation.

Indexed as

AMP-Activated Protein KinasesAnimalsCell PolarityMicrotubule-Associated ProteinsMicrotubulesNeoplasm ProteinsPhenotypePhosphorylationProtein KinasesSignal TransductionTubulinAMP-Activated Protein Kinasescytoplasmic linker protein 170Microtubule-Associated ProteinsNeoplasm ProteinsProtein KinasesTubulin

Identifiers

PMID20495555
OpenAlexW2081289502

What OpenQuestion holds

Textmetadata
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.