Evidence map›Paper›PMID 24379352›Full record

ArticleDiabetes2014

HSP72 is a mitochondrial stress sensor critical for Parkin action, oxidative metabolism, and insulin sensitivity in skeletal muscle.

Brian G Drew, Vicente Ribas, Jamie A Le, Darren C Henstridge, Jennifer Phun, Zhenqi Zhou, Teo Soleymani, Pedram Daraei, Daniel Sitz, Laurent Vergnes and 4 more

Open access · hybridAbstract read
In one paragraph

Article in Diabetes, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 79 papers.

0numbers the graph read from it
0cells of the map it votes in
79citing papers in PubMed
4.3field-weighted citation impact, top 5% 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

79 citing papers in PubMed, 139 citations in OpenAlex.

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  18. Mitophagy for cardioprotection.Basic research in cardiology · 2023
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19 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

14 authors at 2 institutions in 2 countries.

Brian G DrewDavid Geffen School of Medicine, Department of Medicine, Division of Endocrinology, Diabetes and Hypertension, University of California, Los Angeles, Los Angeles, CA.
Vicente Ribas
Jamie A Le
Darren C Henstridge
Jennifer Phun
Zhenqi Zhou
Teo Soleymani
Pedram Daraei
Daniel Sitz
Laurent Vergnes
Jonathan Wanagat
Karen Reue
Mark A Febbraio
Andrea L Hevener
University of California, Los Angeles · USBaker Heart and Diabetes Institute · AU

Funding

Systems genomics of metabolic syndrome traitsP01HL028481 · NHLBI · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI PELLEGRINI, MATTEO · 1985 to 2019
$50.2M
Transgenic & Knock-out MouseP30DK063491 · NIDDK · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI PETER J TONTONOZ · 2003 to 2026
$40.4M
The Lipin Protein Family and Triglyceride Metabolism P01HL090553 · NHLBI · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI YOUNG, STEPHEN G. · 2008 to 2018
$23.3M
The impact of HSP72 on mitochondrial function and muscle metabolismR01DK078760 · NIDDK · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI Andrea L Hevener · 2009 to 2026
$2.8M
ERalpha and the metabolic syndromeR01DK089109 · NIDDK · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI HEVENER, ANDREA L · 2011 to 2014
$1.4M
Mitochondrial genetics in skeletal muscle agingK08AG032873 · NIA · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI WANAGAT, JONATHAN · 2009 to 2013
$473k
XF24-3 Extracellular Flux AnalyzerS10RR026744 · NCRR · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI REUE, KAREN · 2010 to 2010
$168k
NCRR NIH HHS S10 RR026744NCRR NIH HHS S10RR026744NHLBI NIH HHS HL28481NHLBI NIH HHS P01 HL028481NHLBI NIH HHS P01 HL090553NIDDK NIH HHS DK-063491NIDDK NIH HHS DK-078760NIDDK NIH HHS P30 DK063491NIDDK NIH HHS R01 DK078760NIDDK NIH HHS R01 DK089109
6 · The paper itself

Abstract

Increased heat shock protein (HSP) 72 expression in skeletal muscle prevents obesity and glucose intolerance in mice, although the underlying mechanisms of this observation are largely unresolved. Herein we show that HSP72 is a critical regulator of stress-induced mitochondrial triage signaling since Parkin, an E3 ubiquitin ligase known to regulate mitophagy, was unable to ubiquitinate and control its own protein expression or that of its central target mitofusin (Mfn) in the absence of HSP72. In wild-type cells, we show that HSP72 rapidly translocates to depolarized mitochondria prior to Parkin recruitment and immunoprecipitates with both Parkin and Mfn2 only after specific mitochondrial insult. In HSP72 knockout mice, impaired Parkin action was associated with retention of enlarged, dysmorphic mitochondria and paralleled by reduced muscle respiratory capacity, lipid accumulation, and muscle insulin resistance. Reduced oxygen consumption and impaired insulin action were recapitulated in Parkin-null myotubes, confirming a role for the HSP72-Parkin axis in the regulation of muscle insulin sensitivity. These data suggest that strategies to maintain HSP72 may provide therapeutic benefit to enhance mitochondrial quality and insulin action to ameliorate complications associated with metabolic diseases, including type 2 diabetes.

Indexed as

AnimalsCell RespirationHEK293 CellsHSP72 Heat-Shock ProteinsHumansInsulinInsulin ResistanceLipid MetabolismMiceMice, KnockoutMitochondriaMuscle, SkeletalOxidative StressOxygen ConsumptionReactive Oxygen SpeciesUbiquitin-Protein LigasesHSP72 Heat-Shock ProteinsInsulinparkin proteinReactive Oxygen SpeciesUbiquitin-Protein Ligases

Identifiers

PMID24379352
PMCPMC3994950
OpenAlexW2098703027

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.