Evidence map›Paper›PMID 17178908›Full record

ArticleThe Journal of cell biology2006

Chaperone-mediated coupling of endoplasmic reticulum and mitochondrial Ca2+ channels.

György Szabadkai, Katiuscia Bianchi, Péter Várnai, Diego De Stefani, Mariusz R Wieckowski, Dario Cavagna, Anikó I Nagy, Tamás Balla, Rosario Rizzuto

Abstract read
In one paragraph

Article in The Journal of cell biology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 785 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
785citing papers in PubMed, 2 pooled it
–field-weighted citation impact
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

785 citing papers in PubMed, 2 syntheses or guidelines pooled it.

  1. Pooled it
  2. Stay in touch with the endoplasmic reticulum.Science China. Life sciences · 2024
    Pooled it
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725 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

9 authors.

György SzabadkaiDepartment of Experimental and Diagnostic Medicine, Section of General Pathology, Interdisciplinary Center for the Study of Inflammation, Emilia Romagna Laboratory for Genomics and Biotechnology, University of Ferrara, Ferrara 44100, Italy.
Katiuscia Bianchi
Péter Várnai
Diego De Stefani
Mariusz R Wieckowski
Dario Cavagna
Anikó I Nagy
Tamás Balla
Rosario Rizzuto

Funding

Phosphoinositide-calcium Signaling In Cell RegulationZIAHD000196 · NICHD · EUNICE KENNEDY SHRIVER NATIONAL INSTITUTE OF CHILD HEALTH & HUMAN DEVELOPMENT · PI BALLA, TAMAS · 2009 to 2025
$26.3M
PHOSPHOINOSITIDE-CALCIUM SIGNALING IN CELL REGULATIONZ01HD000196 · NICHD · EUNICE KENNEDY SHRIVER NATIONAL INSTITUTE OF CHILD HEALTH & HUMAN DEVELOPMENT · PI BALLA, TAMAS · 1998 to 2008
$1.9M
Telethon GGP05284
6 · The paper itself

Abstract

The voltage-dependent anion channel (VDAC) of the outer mitochondrial membrane mediates metabolic flow, Ca(2+), and cell death signaling between the endoplasmic reticulum (ER) and mitochondrial networks. We demonstrate that VDAC1 is physically linked to the endoplasmic reticulum Ca(2+)-release channel inositol 1,4,5-trisphosphate receptor (IP(3)R) through the molecular chaperone glucose-regulated protein 75 (grp75). Functional interaction between the channels was shown by the recombinant expression of the ligand-binding domain of the IP(3)R on the ER or mitochondrial surface, which directly enhanced Ca(2+) accumulation in mitochondria. Knockdown of grp75 abolished the stimulatory effect, highlighting chaperone-mediated conformational coupling between the IP(3)R and the mitochondrial Ca(2+) uptake machinery. Because organelle Ca(2+) homeostasis influences fundamentally cellular functions and death signaling, the central location of grp75 may represent an important control point of cell fate and pathogenesis.

Indexed as

AequorinAnimalsCalciumCalcium SignalingEndoplasmic ReticulumHeLa CellsHSP70 Heat-Shock ProteinsHumansInositol 1,4,5-TrisphosphateInositol 1,4,5-Trisphosphate ReceptorsLiverMembrane ProteinsMiceMitochondriaMolecular ChaperonesProtein ConformationAequorinCalciumglucose-regulated proteinsHSP70 Heat-Shock ProteinsInositol 1,4,5-TrisphosphateInositol 1,4,5-Trisphosphate ReceptorsMembrane ProteinsMolecular ChaperonesVDAC1 protein, humanVdac1 protein, ratVoltage-Dependent Anion Channel 1

Identifiers

PMID17178908
PMCPMC2064700

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.