The nucleolar phase of signal recognition particle assembly.
Fiche publication
Date publication
août 2024
Journal
Life science alliance
Auteurs
Membres identifiés du Cancéropôle Est :
Dr MASSENET Séverine
Tous les auteurs :
Issa A, Schlotter F, Flayac J, Chen J, Wacheul L, Philippe M, Sardini L, Mostefa L, Vandermoere F, Bertrand E, Verheggen C, Lafontaine DL, Massenet S
Lien Pubmed
Résumé
The signal recognition particle is essential for targeting transmembrane and secreted proteins to the endoplasmic reticulum. Remarkably, because they work together in the cytoplasm, the SRP and ribosomes are assembled in the same biomolecular condensate: the nucleolus. How important is the nucleolus for SRP assembly is not known. Using quantitative proteomics, we have investigated the interactomes of SRP components. We reveal that SRP proteins are associated with scores of nucleolar proteins important for ribosome biogenesis and nucleolar structure. Having monitored the subcellular distribution of SRP proteins upon controlled nucleolar disruption, we conclude that an intact organelle is required for their proper localization. Lastly, we have detected two SRP proteins in Cajal bodies, which indicates that previously undocumented steps of SRP assembly may occur in these bodies. This work highlights the importance of a structurally and functionally intact nucleolus for efficient SRP production and suggests that the biogenesis of SRP and ribosomes may be coordinated in the nucleolus by common assembly factors.
Mots clés
Signal Recognition Particle, metabolism, Cell Nucleolus, metabolism, Ribosomes, metabolism, Humans, Proteomics, methods, Nuclear Proteins, metabolism, Coiled Bodies, metabolism, HeLa Cells, Endoplasmic Reticulum, metabolism
Référence
Life Sci Alliance. 2024 08;7(8):