Evidence map›Paper›PMID 29187525›Full record

ArticleThe Journal of cell biology2018

Humanin is an endogenous activator of chaperone-mediated autophagy.

Zhenwei Gong, Inmaculada Tasset, Antonio Diaz, Jaime Anguiano, Emir Tas, Lingguang Cui, Regina Kuliawat, Honghai Liu, Bernhard Kühn, Ana Maria Cuervo and 1 more

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 67 papers.

0numbers the graph read from it
0cells of the map it votes in
67citing papers in PubMed
7.5field-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

67 citing papers in PubMed, 88 citations in OpenAlex.

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  13. Mechanisms and implications of podocyte autophagy in chronic kidney disease.American journal of physiology. Renal physiology · 2024
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7 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

11 authors at 2 institutions in 1 country.

Zhenwei GongDepartment of Pediatrics, Children's Hospital of Pittsburgh of University of Pittsburgh Medical Center, University of Pittsburgh School of Medicine, Pittsburgh, PA.
Inmaculada TassetDepartment of Developmental and Molecular Biology, Albert Einstein College of Medicine, Bronx, NY.
Antonio DiazDepartment of Developmental and Molecular Biology, Albert Einstein College of Medicine, Bronx, NY.
Jaime AnguianoDepartment of Developmental and Molecular Biology, Albert Einstein College of Medicine, Bronx, NY.
Emir TasDepartment of Pediatrics, Children's Hospital of Pittsburgh of University of Pittsburgh Medical Center, University of Pittsburgh School of Medicine, Pittsburgh, PA.ORCID 0000-0003-3759-2778
Lingguang CuiDepartment of Pediatrics, Albert Einstein College of Medicine, Bronx, NY.
Regina KuliawatDepartment of Developmental and Molecular Biology, Albert Einstein College of Medicine, Bronx, NY.ORCID 0000-0001-8386-2279
Honghai LiuDepartment of Pediatrics, Children's Hospital of Pittsburgh of University of Pittsburgh Medical Center, University of Pittsburgh School of Medicine, Pittsburgh, PA.
Bernhard KühnDepartment of Pediatrics, Children's Hospital of Pittsburgh of University of Pittsburgh Medical Center, University of Pittsburgh School of Medicine, Pittsburgh, PA.
Ana Maria CuervoDepartment of Developmental and Molecular Biology, Albert Einstein College of Medicine, Bronx, NY ana-maria.cuervo@einstein.yu.edu.ORCID 0000-0002-0771-700X
Radhika MuzumdarDepartment of Pediatrics, Children's Hospital of Pittsburgh of University of Pittsburgh Medical Center, University of Pittsburgh School of Medicine, Pittsburgh, PA radhika.muzumdar@chp.edu.ORCID 0000-0003-0284-5536
Albert Einstein College of Medicine · USChildren's Hospital of Pittsburgh · US

Funding

Role of Autophagy in T Cell Function and Immunosenescence (Project 3)P01AG031782 · NIA · ALBERT EINSTEIN COLLEGE OF MEDICINE, INC · PI CUERVO, ANA MARIA · 2009 to 2024
$36.2M
Translational Research CoreP30DK020541 · NIDDK · ALBERT EINSTEIN COLLEGE OF MEDICINE, INC · PI STREAMSON C CHUA · 2015 to 2026
$27.7M
Special Animal CoreP30DK041296 · NIDDK · YESHIVA UNIVERSITY · PI GUPTA, SANJEEV · 1989 to 2018
$22.9M
Einstein's Nathan Shock Center of Excellence in Basic Biology of AgingP30AG038072 · NIA · ALBERT EINSTEIN COLLEGE OF MEDICINE, INC · PI HUFFMAN, DEREK MAJOR · 2010 to 2024
$10.8M
Control of vesicular trafficking in the hepatocyte.R01DK098408 · NIDDK · ALBERT EINSTEIN COLLEGE OF MEDICINE, INC · PI CUERVO, ANA MARIA, WOLKOFF, ALLAN W · 2013 to 2022
$5.6M
Decreased Protein Degradation in AgingR37AG021904 · NIA · ALBERT EINSTEIN COLLEGE OF MEDICINE, INC · PI CUERVO, ANA MARIA · 2013 to 2022
$4.4M
DECREASED PROTEIN DEGRADATION IN AGINGR01AG021904 · NIA · YESHIVA UNIVERSITY · PI CUERVO, ANA MARIA · 2003 to 2012
$3.7M
Understanding Alzheimer's Disease in the Context of the Aging BrainRF1AG054108 · NIA · ALBERT EINSTEIN COLLEGE OF MEDICINE, INC · PI CUERVO, ANA MARIA · 2016 to 2016
$2.1M
Novel Regulators of Glucose Homeostasis in AgingR01AG035114 · NIA · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI MUZUMDAR, RADHIKA HIREN · 2010 to 2014
$1.6M
Novel Mitochondria-Associated Peptide and Beta Cell Function in AgingR56AG044519 · NIA · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI MUZUMDAR, RADHIKA HIREN · 2015 to 2015
$385k
NIA NIH HHS P01 AG031782NIA NIH HHS P30 AG038072NIA NIH HHS R01 AG021904NIA NIH HHS R01 AG035114NIA NIH HHS R37 AG021904NIA NIH HHS R56 AG044519NIA NIH HHS RF1 AG054108NIDDK NIH HHS P30 DK020541NIDDK NIH HHS P30 DK041296NIDDK NIH HHS R01 DK098408
6 · The paper itself

Abstract

Chaperone-mediated autophagy (CMA) serves as quality control during stress conditions through selective degradation of cytosolic proteins in lysosomes. Humanin (HN) is a mitochondria-associated peptide that offers cytoprotective, cardioprotective, and neuroprotective effects in vivo and in vitro. In this study, we demonstrate that HN directly activates CMA by increasing substrate binding and translocation into lysosomes. The potent HN analogue HNG protects from stressor-induced cell death in fibroblasts, cardiomyoblasts, neuronal cells, and primary cardiomyocytes. The protective effects are lost in CMA-deficient cells, suggesting that they are mediated through the activation of CMA. We identified that a fraction of endogenous HN is present at the cytosolic side of the lysosomal membrane, where it interacts with heat shock protein 90 (HSP90) and stabilizes binding of this chaperone to CMA substrates as they bind to the membrane. Inhibition of HSP90 blocks the effect of HNG on substrate translocation and abolishes the cytoprotective effects. Our study provides a novel mechanism by which HN exerts its cardioprotective and neuroprotective effects.

Indexed as

AutophagyAnimalsCells, CulturedCell SurvivalCytosolHSP90 Heat-Shock ProteinsIntracellular Signaling Peptides and ProteinsLysosomesMaleMiceMolecular ChaperonesNIH 3T3 CellsRatsRats, WistarHSP90 Heat-Shock ProteinshumaninIntracellular Signaling Peptides and ProteinsMolecular Chaperones

Identifiers

PMID29187525
PMCPMC5800795
OpenAlexW2770440873

What OpenQuestion holds

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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.