Evidence map›Paper›PMID 16505167›Full record

ArticleThe Journal of cell biology2006

Autophagy-mediated clearance of huntingtin aggregates triggered by the insulin-signaling pathway.

Ai Yamamoto, M Laura Cremona, James E Rothman

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 190 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
190citing papers in PubMed, 1 pooled it
11.7field-weighted citation impact, top 1% 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

190 citing papers in PubMed, 1 synthesis or guideline pooled it, 362 citations in OpenAlex.

  1. Guideline
  2. Review
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  8. Review
  9. Review
  10. Huntingtin contains an ubiquitin-binding domain and regulates lysosomal targeting of mitochondrial and RNA-binding proteins.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  11. Review
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Macroautophagy in CNS health and disease.Nature reviews. Neuroscience · 2022
    Review
  20. Article

130 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

3 authors at 1 institution in 1 country.

Ai YamamotoThe Judith P. Sulzberger Columbia Genome Center, Department of Physiology and Cellular Biophysics, Columbia University, New York, NY 10032, USA.
M Laura Cremona
James E Rothman
Columbia University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Conditional mouse models of polyglutamine diseases, such as Huntington's disease (HD), have revealed that cells can clear accumulated pathogenic proteins if the continuous production of the mutant transgene is halted. Invariably, the clearance of the protein leads to regression of the disease symptoms in mice. In light of these findings, it is critical to determine the pathway responsible for alleviating this protein accumulation to define targets to fight these diseases. In a functional genetic screen of HD, we found that activation of insulin receptor substrate-2, which mediates the signaling cascades of insulin and insulin-like growth factor 1, leads to a macroautophagy-mediated clearance of the accumulated proteins. The macroautophagy is triggered despite activation of Akt, mammalian target of rapamycin (mTOR), and S6 kinase, but still requires proteins previously implicated in macroautophagy, such as Beclin1 and hVps34. These findings indicate that the accumulation of mutant protein can lead to mTOR-independent macroautophagy and that lysosome-mediated degradation of accumulated protein differs from degradation under conditions of starvation.

Indexed as

AnimalsApoptosis Regulatory ProteinsAutophagyBeclin-1Cell LineGene Expression ProfilingHuntingtin ProteinInsulinInsulin Receptor Substrate ProteinsIntracellular Signaling Peptides and ProteinsMiceMutationNerve Tissue ProteinsNuclear ProteinsPhosphatidylinositol 3-KinasesPhosphoproteinsApoptosis Regulatory ProteinsBeclin-1Becn1 protein, mouseHtt protein, mouseHuntingtin ProteinInsulinInsulin Receptor Substrate ProteinsIntracellular Signaling Peptides and ProteinsIrs2 protein, mouseNerve Tissue ProteinsNuclear ProteinsPhosphatidylinositol 3-KinasesPhosphoproteinsProteinsRNA, Small Interfering

Identifiers

PMID16505167
PMCPMC2063704
OpenAlexW2154404753

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.