Evidence map›Paper›PMID 36050837›Full record

ArticleThe Plant journal : for cell and molecular biology2022

FRIENDLY (FMT) is an RNA binding protein associated with cytosolic ribosomes at the mitochondrial surface.

Mickaele Hemono, Thalia Salinas-Giegé, Jeanne Roignant, Audrey Vingadassalon, Philippe Hammann, Elodie Ubrig, Patryk Ngondo, Anne-Marie Duchêne

Open access · hybridAbstract read
In one paragraph

Article in The Plant journal : for cell and molecular biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
1.1field-weighted citation impact, top 23% 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

8 citing papers in PubMed, 15 citations in OpenAlex.

  1. Review
  2. TheProceedings of the National Academy of Sciences of the United States of America · 2026
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

8 authors at 1 institution in 1 country.

Mickaele HemonoInstitut de biologie moléculaire des plantes, UPR 2357 du CNRS, Université de Strasbourg, 12 rue du Général Zimmer, 67084, Strasbourg Cedex, France.
Thalia Salinas-GiegéInstitut de biologie moléculaire des plantes, UPR 2357 du CNRS, Université de Strasbourg, 12 rue du Général Zimmer, 67084, Strasbourg Cedex, France.
Jeanne RoignantInstitut de biologie moléculaire des plantes, UPR 2357 du CNRS, Université de Strasbourg, 12 rue du Général Zimmer, 67084, Strasbourg Cedex, France.
Audrey VingadassalonInstitut de biologie moléculaire des plantes, UPR 2357 du CNRS, Université de Strasbourg, 12 rue du Général Zimmer, 67084, Strasbourg Cedex, France.
Philippe HammannPlateforme Protéomique Strasbourg-Esplanade, Institut de Biologie Moléculaire et Cellulaire, FR1589 du CNRS, 2 Allée Konrad Roentgen, 67084, Strasbourg Cedex, France.ORCID 0000-0002-6883-9203
Elodie UbrigInstitut de biologie moléculaire des plantes, UPR 2357 du CNRS, Université de Strasbourg, 12 rue du Général Zimmer, 67084, Strasbourg Cedex, France.
Patryk NgondoInstitut de biologie moléculaire des plantes, UPR 2357 du CNRS, Université de Strasbourg, 12 rue du Général Zimmer, 67084, Strasbourg Cedex, France.
Anne-Marie DuchêneInstitut de biologie moléculaire des plantes, UPR 2357 du CNRS, Université de Strasbourg, 12 rue du Général Zimmer, 67084, Strasbourg Cedex, France.ORCID 0000-0002-6736-0524
Centre National de la Recherche Scientifique · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The spatial organization of protein synthesis in the eukaryotic cell is essential for maintaining the integrity of the proteome and the functioning of the cell. Translation on free polysomes or on ribosomes associated with the endoplasmic reticulum has been studied for a long time. More recent data have revealed selective translation of mRNAs in other compartments, in particular at the surface of mitochondria. Although these processes have been described in many organisms, particularky in plants, the mRNA targeting and localized translation mechanisms remain poorly understood. Here, the Arabidopsis thaliana Friendly (FMT) protein is shown to be a cytosolic RNA binding protein that associates with cytosolic ribosomes at the surface of mitochondria. FMT knockout delays seedling development and causes mitochondrial clustering. The mutation also disrupts the mitochondrial proteome, as well as the localization of nuclear transcripts encoding mitochondrial proteins at the surface of mitochondria. These data indicate that FMT participates in the localization of mRNAs and their translation at the surface of mitochondria.

Indexed as

ArabidopsisProteomeMitochondriaMitochondrial ProteinsProtein BiosynthesisRibosomesRNA-Binding ProteinsRNA, MessengerMitochondrial ProteinsProteomeRNA-Binding ProteinsRNA, Messengerco-translational importlocalized translationmRNA trafficking

Identifiers

PMID36050837
PMCPMC9826127
OpenAlexW4294176387

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.