The interactome of CLUH reveals its association to SPAG5 and its co-translational proximity to mitochondrial proteins.
BMC Biol
; 20(1): 13, 2022 01 10.
Article
en En
| MEDLINE
| ID: mdl-35012549
ABSTRACT
BACKGROUND:
Mitochondria 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.RESULTS:
Here 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.CONCLUSIONS:
Overall, 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.Palabras clave
Texto completo:
1
Base de datos:
MEDLINE
Asunto principal:
Proteínas de Ciclo Celular
/
Proteínas Mitocondriales
/
Mamíferos
Tipo de estudio:
Risk_factors_studies
Idioma:
En
Revista:
BMC Biol
Asunto de la revista:
BIOLOGIA
Año:
2022
Tipo del documento:
Article