Evidence map›Paper›PMID 20869947›Full record

ArticleBiochemical and biophysical research communications2010

Fast kinase domain-containing protein 3 is a mitochondrial protein essential for cellular respiration.

Maria Simarro, Alfredo Gimenez-Cassina, Nancy Kedersha, Jean-Bernard Lazaro, Guillaume O Adelmant, Jarrod A Marto, Kirsten Rhee, Sarah Tisdale, Nika Danial, Charaf Benarafa and 2 more

Abstract read
In one paragraph

Article in Biochemical and biophysical research communications, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed
0.9field-weighted citation impact, top 27% 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

46 citing papers in PubMed, 76 citations in OpenAlex.

  1. Article
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  7. Upstream open reading frames may contain hundreds of novel human exons.bioRxiv : the preprint server for biology · 2024
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  19. Article
  20. Systematic Analysis of FASTK Gene Family Alterations in Cancer.International journal of molecular sciences · 2021
    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

12 authors at 4 institutions in 3 countries.

Maria SimarroDivision of Rheumatology, Immunology and Allergy, Brigham and Women's Hospital, and Department of Medicine, Harvard Medical School, Boston, MA 02115, United States.
Alfredo Gimenez-Cassina
Nancy Kedersha
Jean-Bernard Lazaro
Guillaume O Adelmant
Jarrod A Marto
Kirsten Rhee
Sarah Tisdale
Nika Danial
Charaf Benarafa
Anonio Orduña
Paul Anderson
Dana-Farber Cancer Institute · USBrigham and Women's Hospital · USHospital Clínico Universitario de Valladolid · ESUniversity of Bern · CH

Funding

Post-transcriptional regulation of inflammatory arthritisP01AI065858 · NIAID · BRIGHAM AND WOMEN'S HOSPITAL · PI LEE, DAVID M · 2006 to 2010
$11.1M
The role of FAST in immune-mediated inflammatory diseaseR01AR051472 · NIAMS · BRIGHAM AND WOMEN'S HOSPITAL · PI ANDERSON, PAUL J. · 2004 to 2008
$1.8M
NIAID NIH HHS P01 AI065858NIAMS NIH HHS R01 AR051472
6 · The paper itself

Abstract

Fas-activated serine/threonine phosphoprotein (FAST) is the founding member of the FAST kinase domain-containing protein (FASTKD) family that includes FASTKD1-5. FAST is a sensor of mitochondrial stress that modulates protein translation to promote the survival of cells exposed to adverse conditions. Mutations in FASTKD2 have been linked to a mitochondrial encephalomyopathy that is associated with reduced cytochrome c oxidase activity, an essential component of the mitochondrial electron transport chain. We have confirmed the mitochondrial localization of FASTKD2 and shown that all FASTKD family members are found in mitochondria. Although human and mouse FASTKD1-5 genes are expressed ubiquitously, some of them are most abundantly expressed in mitochondria-enriched tissues. We have found that RNA interference-mediated knockdown of FASTKD3 severely blunts basal and stress-induced mitochondrial oxygen consumption without disrupting the assembly of respiratory chain complexes. Tandem affinity purification reveals that FASTKD3 interacts with components of mitochondrial respiratory and translation machineries. Our results introduce FASTKD3 as an essential component of mitochondrial respiration that may modulate energy balance in cells exposed to adverse conditions by functionally coupling mitochondrial protein synthesis to respiration.

Indexed as

Cell RespirationAnimalsGene Knockdown TechniquesHeLa CellsHumansMiceMice, Inbred C57BLMitochondriaMitochondrial ProteinsProtein Serine-Threonine KinasesRNA InterferenceFASTKD3 protein, humanFASTKD3 protein, mouseMitochondrial ProteinsProtein Serine-Threonine Kinases

Identifiers

PMID20869947
PMCPMC2963690
OpenAlexW1993853380

What OpenQuestion holds

Textmetadata
LicenceTDM
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.