Publications by authors named "Marina Cerqua"
Cancer cells rely on invasive growth to survive in a hostile microenvironment; this growth is characterised by interconnected processes such as epithelial-to-mesenchymal transition and migration. A master regulator of these events is the MET oncogene, which is overexpressed in the majority of cancers; however, since mutations in the MET oncogene are seen only rarely in cancers and are relatively infrequent, the mechanisms that cause this widespread MET overexpression remain obscure. Here, we show that the 5' untranslated region (5'UTR) of MET mRNA harbours two functional stress-responsive elements, conferring translational regulation by the integrated stress response (ISR), regulated by phosphorylation of eukaryotic translation initiation factor 2 alpha (eIF2α) at serine 52.
View Article and Find Full Text PDFArticle Synopsis
- The MET oncogene's tyrosine kinase receptor has an extracellular domain called PSI, which has been previously unexplored in terms of function despite being evolutionarily conserved.
- Recent experiments reveal that the MET extracellular PSI domain exhibits disulfide isomerase activity, crucial for the maturation process of the MET precursor protein into its active forms, which are involved in signaling pathways.
- Mutations in the PSI domain hinder the cleavage and maturation of the MET protein, leading to its accumulation in the Golgi apparatus and preventing essential biological processes triggered by its ligand, Hepatocyte Growth Factor (HGF).
is an oncogene encoding the tyrosine kinase receptor for hepatocyte growth factor (HGF). Upon ligand binding, MET activates multiple signal transducers, including PI3K/AKT, STAT3, and MAPK. When mutated or amplified, becomes a "driver" for the onset and progression of cancer.
View Article and Find Full Text PDF