Evidence map›Paper›PMID 35883436›Full record

ReviewBiomolecules2022

The Mitochondrial HSP90 Paralog TRAP1: Structural Dynamics, Interactome, Role in Metabolic Regulation, and Inhibitors.

Abhinav Joshi, Takeshi Ito, Didier Picard, Len Neckers

Open access · goldAbstract readReview
In one paragraph

Review in Biomolecules, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
2.7field-weighted citation impact, top 9% 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

23 citing papers in PubMed, 34 citations in OpenAlex.

  1. Review
  2. Article
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  4. Review
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  7. Review
  8. Review
  9. Article
  10. Article
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  12. Preparation of DOX-TPP/HA-ss-OA Nanoparticles, Investigation of Drug Release BehaviorCombinatorial chemistry & high throughput screening · 2025
    Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Review
  18. Article
  19. Complex II ambiguities-FADHThe Journal of biological chemistry · 2024
    Review
  20. Article
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

4 authors at 2 institutions in 2 countries.

Abhinav JoshiUrologic Oncology Branch, Center for Cancer Research, National Cancer Institute (NCI), Bethesda, MD 20892, USA.ORCID 0000-0002-1417-6918
Takeshi ItoUrologic Oncology Branch, Center for Cancer Research, National Cancer Institute (NCI), Bethesda, MD 20892, USA.ORCID 0000-0002-9741-4984
Didier PicardDepartment of Molecular and Cellular Biology, Université de Genève, Sciences III, 30 Quai Ernest-Ansermet, CH-1211 Geneva, Switzerland.ORCID 0000-0001-8816-9668
Len NeckersUrologic Oncology Branch, Center for Cancer Research, National Cancer Institute (NCI), Bethesda, MD 20892, USA.
National Cancer Institute · USUniversity of Geneva · CH

Funding

Role of HSP90 Family Chaperone Proteins in Cellular Signal TransductionZIASC010074 · NCI · DIVISION OF CLINICAL SCIENCES - NCI · PI NECKERS, LEONARD · 2009 to 2025
$13.3M
Intramural NIH HHS ZIA SC010074
6 · The paper itself

Abstract

The HSP90 paralog TRAP1 was discovered more than 20 years ago; yet, a detailed understanding of the function of this mitochondrial molecular chaperone remains elusive. The dispensable nature of TRAP1 in vitro and in vivo further complicates an understanding of its role in mitochondrial biology. TRAP1 is more homologous to the bacterial HSP90, HtpG, than to eukaryotic HSP90. Lacking co-chaperones, the unique structural features of TRAP1 likely regulate its temperature-sensitive ATPase activity and shed light on the alternative mechanisms driving the chaperone's nucleotide-dependent cycle in a defined environment whose physiological temperature approaches 50 °C. TRAP1 appears to be an important bioregulator of mitochondrial respiration, mediating the balance between oxidative phosphorylation and glycolysis, while at the same time promoting mitochondrial homeostasis and displaying cytoprotective activity. Inactivation/loss of TRAP1 has been observed in several neurodegenerative diseases while TRAP1 expression is reported to be elevated in multiple cancers and, as with HSP90, evidence of addiction to TRAP1 has been observed. In this review, we summarize what is currently known about this unique HSP90 paralog and why a better understanding of TRAP1 structure, function, and regulation is likely to enhance our understanding of the mechanistic basis of mitochondrial homeostasis.

Indexed as

HSP90 Heat-Shock ProteinsMitochondriaGlycolysisHomeostasisMolecular ChaperonesOxidative PhosphorylationHSP90 Heat-Shock ProteinsMolecular ChaperonesHSP90metabolismmitochondriamolecular chaperoneOxPhostetramersTRAP1

Identifiers

PMID35883436
PMCPMC9312948
OpenAlexW4283450523

What Socratic holds

Textmetadata
LicenceCC BY
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 Socratic graph.