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Analyses of FBXL6 interaction with newly synthesized proteins.

ABSTRACT: HEK cells were grown in light media for two weeks. One day before experiments, cells were transfected with FBXL6-flag or B-gal (control). At t=0, cells were switched to heavy media for 3h and then Flag immunoprecipitation were performed. Pulled down protein were analyzed by mass spectrometry.

INSTRUMENT(S): Orbitrap Fusion Lumos

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Dupuy Jean-William

LAB HEAD: Giovanni Bénard

PROVIDER: PXD037602 | Pride | 2023-09-25

REPOSITORIES: Pride

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The E3 ubiquitin ligase FBXL6 controls the quality of newly synthesized mitochondrial ribosomal proteins.

Lavie Julie J Lalou Claude C Mahfouf Walid W Dupuy Jean-William JW Lacaule Aurélie A Cywinska Agata Ars AA Lacombe Didier D Duchêne Anne-Marie AM Raymond Anne-Aurélie AA Rezvani Hamid Reza HR Ngondo Richard Patryk RP Bénard Giovanni G

Cell reports 20230601 6

In mammals, about 99% of mitochondrial proteins are synthesized in the cytosol as precursors that are subsequently imported into the organelle. The mitochondrial health and functions rely on an accurate quality control of these imported proteins. Here, we show that the E3 ubiquitin ligase F box/leucine-rich-repeat protein 6 (FBXL6) regulates the quality of cytosolically translated mitochondrial proteins. Indeed, we found that FBXL6 substrates are newly synthesized mitochondrial ribosomal protein ...[more]

PMID: 37267103

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