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PXD061930

PXD061930 is an original dataset announced via ProteomeXchange.

Dataset Summary
TitleThe Arabidopsis FRIENDLY (FMT) protein interacts with NAC and determines where nuclear-encoded mitochondrial proteins are translated
DescriptionMitochondria are not only the powerhouses of the cell. They are also dynamic signaling hubs, playing a key role in cellular metabolism and adaptation. Proper mitochondrial function depends largely on the import of proteins encoded by the nucleus. Using RNA immunoprecipitation and proximity labeling (TurboID), we show that Arabidopsis thaliana FRIENDLY (FMT) protein specifically recognizes the mRNAs of several organellar-destined proteins, mostly mitochondrial, and is in close proximity to these proteins during their translation. Remarkably, when FMT is absent, its target mRNAs lose their correct cellular localization. Our TurboID approach also confirms the interaction between FMT and the Nascent polypeptide Associated Complex (NAC), a ribosome-associated platform involved in the maturation and sorting of nascent peptides. Taken together, these results suggest that FMT, through its interaction with NAC and the ribosome, is involved in the spatial regulation of translation in the cell. FMT itself is under tight cellular control. It is rapidly degraded under stress but is overproduced in specific conditions, such as germination, impacting mitochondrial activity. Since mitochondria act as signaling hubs, this regulation of FMT could help the cell to quickly adapt to changing environments.
HostingRepositoryPRIDE
AnnounceDate2026-03-05
AnnouncementXMLSubmission_2026-03-05_01:24:33.652.xml
DigitalObjectIdentifierhttps://dx.doi.org/10.6019/PXD061930
ReviewLevelPeer-reviewed dataset
DatasetOriginOriginal dataset
RepositorySupportSupported dataset by repository
PrimarySubmitterJohana Chicher
SpeciesList scientific name: Arabidopsis thaliana (Mouse-ear cress); NCBI TaxID: NEWT:3702;
ModificationListphosphorylated residue; acetylated residue; monohydroxylated residue; iodoacetamide derivatized residue
InstrumentQ Exactive Plus
Dataset History
RevisionDatetimeStatusChangeLog Entry
02025-03-17 09:16:30ID requested
12026-03-05 01:24:34announced
Publication List
10.6019/PXD061930;
10.1073/PNAS.2521483123;
Keyword List
submitter keyword: None
Contact List
Anne-Marie Duchêne
contact affiliationInstitut de biologie moléculaire des plantes, UPR 2357 du CNRS, Université de Strasbourg, 12 rue du Général Zimmer, 67084 Strasbourg cedex, France
contact emailanne-marie.duchene@ibmp-cnrs.unistra.fr
lab head
Johana Chicher
contact affiliationUniversité de Strasbourg, Plateforme Protéomique Strasbourg-Esplanade, Centre National de la Recherche Scientifique
contact emailj.chicher@ibmc-cnrs.unistra.fr
dataset submitter
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