Evidence map›Paper›PMID 21979464›Full record

ArticleCell death and differentiation2012

TRAP1 and the proteasome regulatory particle TBP7/Rpt3 interact in the endoplasmic reticulum and control cellular ubiquitination of specific mitochondrial proteins.

M R Amoroso, D S Matassa, G Laudiero, A V Egorova, R S Polishchuk, F Maddalena, A Piscazzi, S Paladino, D Sarnataro, C Garbi and 2 more

Open access · bronzeAbstract read
In one paragraph

Article in Cell death and differentiation, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.

0numbers the graph read from it
0cells of the map it votes in
58citing papers in PubMed
2.5field-weighted citation impact, top 12% 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

58 citing papers in PubMed, 96 citations in OpenAlex.

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  20. TRAP1 in Oxidative Stress and Neurodegeneration.Antioxidants (Basel, Switzerland) · 2021
    Review
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

12 authors at 4 institutions in 1 country.

M R AmorosoDepartment of Biochemistry and Medical Biotechnologies, University of Naples Federico II, Via Pansini 5, Naples 80131, Italy.
D S Matassa
G Laudiero
A V Egorova
R S Polishchuk
F Maddalena
A Piscazzi
S Paladino
D Sarnataro
C Garbi
M Landriscina
F Esposito
University of Naples Federico II · ITTelethon Institute Of Genetics And Medicine · ITUniversity of Foggia · ITIstituti di Ricovero e Cura a Carattere Scientifico · IT

Funding

Telethon GTF08001
6 · The paper itself

Abstract

Tumor necrosis factor receptor-associated protein-1 (TRAP1) is a mitochondrial (MITO) antiapoptotic heat-shock protein. The information available on the TRAP1 pathway describes just a few well-characterized functions of this protein in mitochondria. However, our group's use of mass-spectrometric analysis identified TBP7, an AAA-ATPase of the 19S proteasomal subunit, as a putative TRAP1-interacting protein. Surprisingly, TRAP1 and TBP7 colocalize in the endoplasmic reticulum (ER), as demonstrated by biochemical and confocal/electron microscopic analyses, and interact directly, as confirmed by fluorescence resonance energy transfer analysis. This is the first demonstration of TRAP1's presence in this cellular compartment. TRAP1 silencing by short-hairpin RNAs, in cells exposed to thapsigargin-induced ER stress, correlates with upregulation of BiP/Grp78, thus suggesting a role of TRAP1 in the refolding of damaged proteins and in ER stress protection. Consistently, TRAP1 and/or TBP7 interference enhanced stress-induced cell death and increased intracellular protein ubiquitination. These experiments led us to hypothesize an involvement of TRAP1 in protein quality control for mistargeted/misfolded mitochondria-destined proteins, through interaction with the regulatory proteasome protein TBP7. Remarkably, expression of specific MITO proteins decreased upon TRAP1 interference as a consequence of increased ubiquitination. The proposed TRAP1 network has an impact in vivo, as it is conserved in human colorectal cancers, is controlled by ER-localized TRAP1 interacting with TBP7 and provides a novel model of the ER-mitochondria crosstalk.

Indexed as

Endoplasmic Reticulum StressUbiquitinationATPases Associated with Diverse Cellular ActivitiesCell Line, TumorColorectal NeoplasmsEndoplasmic ReticulumEndoplasmic Reticulum Chaperone BiPGene SilencingHSP90 Heat-Shock ProteinsHumansMitochondrial ProteinsNeoplasm ProteinsProteasome Endopeptidase ComplexProtein FoldingATPases Associated with Diverse Cellular ActivitiesEndoplasmic Reticulum Chaperone BiPHSP90 Heat-Shock ProteinsHSPA5 protein, humanMitochondrial ProteinsNeoplasm ProteinsProteasome Endopeptidase ComplexPSMC4 protein, humanTRAP1 protein, human

Identifiers

PMID21979464
PMCPMC3307973
OpenAlexW2130461458

What OpenQuestion holds

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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.