Evidence map›Paper›PMID 30821613›Full record

ArticleAutophagy2019

Targetome analysis of chaperone-mediated autophagy in cancer cells.

Yuqing Hao, Merve Kacal, Amanda Tomie Ouchida, Boxi Zhang, Erik Norberg, Helin Vakifahmetoglu-Norberg

Open access · hybridAbstract read
In one paragraph

Article in Autophagy, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.

0numbers the graph read from it
0cells of the map it votes in
53citing papers in PubMed
7.8field-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

53 citing papers in PubMed, 85 citations in OpenAlex.

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  12. 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
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  14. Autophagy · 2024
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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

6 authors at 1 institution in 1 country.

Yuqing Haoa Department of Physiology and Pharmacology, Biomedicum, Karolinska Institutet , Stockholm , Sweden.ORCID 0000-0002-1910-0664
Merve Kacala Department of Physiology and Pharmacology, Biomedicum, Karolinska Institutet , Stockholm , Sweden.
Amanda Tomie Ouchidaa Department of Physiology and Pharmacology, Biomedicum, Karolinska Institutet , Stockholm , Sweden.
Boxi Zhanga Department of Physiology and Pharmacology, Biomedicum, Karolinska Institutet , Stockholm , Sweden.
Erik Norberga Department of Physiology and Pharmacology, Biomedicum, Karolinska Institutet , Stockholm , Sweden.
Helin Vakifahmetoglu-Norberga Department of Physiology and Pharmacology, Biomedicum, Karolinska Institutet , Stockholm , Sweden.
Karolinska Institutet · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Chaperone-mediated autophagy (CMA) is a lysosomal degradation pathway of select soluble proteins. Nearly one-third of the soluble proteins are predicted to be recognized by this pathway, yet only a minor fraction of this proteome has been identified as CMA substrates in cancer cells. Here, we undertook a quantitative multiplex mass spectrometry approach to study the proteome of isolated lysosomes in cancer cells during CMA-activated conditions. By integrating bioinformatics analyses, we identified and categorized proteins of multiple cellular pathways that were specifically targeted by CMA. Beyond verifying metabolic pathways, we show that multiple components involved in select biological processes, including cellular translation, was specifically targeted for degradation by CMA. In particular, several proteins of the translation initiation complex were identified as

Indexed as

Cell Line, TumorChaperone-Mediated AutophagyDEAD-box RNA HelicasesEukaryotic Initiation Factor-4FEukaryotic Initiation FactorsGene OntologyHSC70 Heat-Shock ProteinsHumansLysosomal-Associated Membrane Protein 2LysosomesNeoplasmsProtein BiosynthesisProteolysisProteomeDDX3X protein, humanDEAD-box RNA HelicasesEIF4H protein, humanEukaryotic Initiation Factor-4FEukaryotic Initiation FactorsHSC70 Heat-Shock ProteinsLysosomal-Associated Membrane Protein 2ProteomeAutophagydegradomelysosomeproteometranslation

Identifiers

PMID30821613
PMCPMC6693453
OpenAlexW2920704435

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.