Evidence map›Paper›PMID 35012549›Full record

ArticleBMC biology2022

The interactome of CLUH reveals its association to SPAG5 and its co-translational proximity to mitochondrial proteins.

Mickaële Hémono, Alexandre Haller, Johana Chicher, Anne-Marie Duchêne, Richard Patryk Ngondo

Open access · goldAbstract read
In one paragraph

Article in BMC biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
2.8field-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

13 citing papers in PubMed, 26 citations in OpenAlex.

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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

5 authors at 1 institution in 1 country.

Mickaële HémonoInstitut de biologie moléculaire des plantes, CNRS, Université de Strasbourg, 12 rue du Général Zimmer, Strasbourg, 67084, France.
Alexandre HallerInstitut de biologie moléculaire des plantes, CNRS, Université de Strasbourg, 12 rue du Général Zimmer, Strasbourg, 67084, France.
Johana ChicherPlateforme protéomique Strasbourg Esplanade FR1589 du CNRS, Université de Strasbourg, Strasbourg, France.
Anne-Marie DuchêneInstitut de biologie moléculaire des plantes, CNRS, Université de Strasbourg, 12 rue du Général Zimmer, Strasbourg, 67084, France.
Richard Patryk NgondoInstitut de biologie moléculaire des plantes, CNRS, Université de Strasbourg, 12 rue du Général Zimmer, Strasbourg, 67084, France. patryk.ngondo@unistra.fr.ORCID 0000-0003-4847-9375
Centre National de la Recherche Scientifique · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundMitochondria require thousands of proteins to fulfill their essential function in energy production and other fundamental biological processes. These proteins are mostly encoded by the nuclear genome, translated in the cytoplasm before being imported into the organelle. RNA binding proteins (RBPs) are central players in the regulation of this process by affecting mRNA translation, stability, or localization. CLUH is an RBP recognizing specifically mRNAs coding for mitochondrial proteins, but its precise molecular function and interacting partners remain undiscovered in mammals.

resultsHere we reveal for the first time CLUH interactome in mammalian cells. Using both co-IP and BioID proximity-labeling approaches, we identify novel molecular partners interacting stably or transiently with CLUH in HCT116 cells and mouse embryonic stem cells. We reveal stable RNA-independent interactions of CLUH with itself and with SPAG5 in cytosolic granular structures. More importantly, we uncover an unexpected proximity of CLUH to mitochondrial proteins and their cognate mRNAs in the cytosol. We show that this interaction occurs during the process of active translation and is dependent on CLUH TPR domain.

conclusionsOverall, through the analysis of CLUH interactome, our study sheds a new light on CLUH molecular function by revealing new partners and by highlighting its link to the translation and subcellular localization of some mRNAs coding for mitochondrial proteins.

Indexed as

MammalsMitochondrial ProteinsAnimalsCell Cycle ProteinsHumansMiceCell Cycle ProteinsMitochondrial ProteinsBioIDCLUHLocalized translationNuclear encoded mitochondrial proteinsProximity labelingRNA binding proteinsSPAG5TranslationTurboID

Identifiers

PMID35012549
PMCPMC8744257
OpenAlexW4206418540

What OpenQuestion holds

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LicenceCC BY
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Registered trials

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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.