title: A new role under sortilin's belt in cancer.
abstract: The neurotensin receptor-3 also known as sortilin was the first member of the small family of vacuolar protein sorting 10 protein domain (Vps10p) discovered two decades ago in the human brain. The expression of sortilin is not confined to the nervous system but sortilin is ubiquitously expressed in many tissues. Sortilin has multiple roles in the cell as a receptor or a co-receptor, in protein transport of many interacting partners to the plasma membrane, to the endocytic pathway and to the lysosomes for protein degradation. Sortilin could be considered as the cells own shuttle system. In many human diseases including neurological diseases and cancer, sortilin expression has been shown to be deregulated. In addition, some studies have highlighted that the extracellular domain of sortilin is shedded into the culture media by an unknown mechanism. Sortilin can be released in exosomes and appears to control some mechanisms of exosome biogenesis. In lung cancer cells, sortilin can associate with two receptor tyrosine kinase receptors called the TES complex found in exosomes. Exosomes carrying the TES complex can convey a microenvironment control through the activation of ErbB signaling pathways and the release of angiogenic factors. Deregulation of sortilin function is now emerging to be implicated in four major human diseases- cardiovascular disease, Type 2 diabetes mellitus, Alzheimer disease and cancer.
authors.affiliation: EA3842 Homéostasie cellulaire et pathologies and Chaire de Pneumologie Expérimentale, Faculté de Médecine, Université de Limoges, Limoges, France; University of Liverpool, Institute of Translational Medicine, Department of Molecular & Clinical Cancer Medicine, Liverpool, UK.
authors.forename: Cornelia M
authors.initials: CM
authors.lastname: Wilson
authors.affiliation: EA3842 Homéostasie cellulaire et pathologies and Chaire de Pneumologie Expérimentale, Faculté de Médecine, Université de Limoges , Limoges, France.
authors.forename: Thomas
authors.initials: T
authors.lastname: Naves
authors.affiliation: EA3842 Homéostasie cellulaire et pathologies and Chaire de Pneumologie Expérimentale, Faculté de Médecine, Université de Limoges , Limoges, France.
authors.forename: Hussein
authors.initials: H
authors.lastname: Al Akhrass
authors.affiliation: EA3842 Homéostasie cellulaire et pathologies and Chaire de Pneumologie Expérimentale, Faculté de Médecine, Université de Limoges, Limoges, France; Service de Pathologie Respiratoire, Center Hospitalier et Universitaire de Limoges, Limoges, France.
authors.forename: François
authors.initials: F
authors.lastname: Vincent
authors.affiliation: Service de Pathologie Respiratoire, Center Hospitalier et Universitaire de Limoges , Limoges, France.
authors.forename: Boris
authors.initials: B
authors.lastname: Melloni
authors.affiliation: Service de Pathologie Respiratoire, Center Hospitalier et Universitaire de Limoges , Limoges, France.
authors.forename: François
authors.initials: F
authors.lastname: Bonnaud
authors.affiliation: EA3842 Homéostasie cellulaire et pathologies and Chaire de Pneumologie Expérimentale, Faculté de Médecine, Université de Limoges , Limoges, France.
authors.forename: Fabrice
authors.initials: F
authors.lastname: Lalloué
authors.affiliation: EA3842 Homéostasie cellulaire et pathologies and Chaire de Pneumologie Expérimentale, Faculté de Médecine, Université de Limoges , Limoges, France.
authors.forename: Marie-Odile
authors.initials: MO
authors.lastname: Jauberteau
keywords: EGFR; TrkB; exosome; lung cancer; sortilin