title: Membrane-bound mucin modular domains: from structure to function.
abstract: Mucins belong to a heterogeneous family of large O-glycoproteins composed of a long peptidic chain called apomucin on which are linked hundreds of oligosaccharidic chains. Among mucins, membrane-bound mucins are modular proteins and have a structural organization usually containing Pro/Thr/Ser-rich O-glycosylated domains (PTS), EGF-like and SEA domains. Via these modular domains, the membrane-bound mucins participate in cell signalling and cell interaction with their environment in normal and pathological conditions. Moreover, the recent knowledge of these domains and their biological activities led to the development of new therapeutic approaches involving mucins. In this review, we show 3D structures of EGF and SEA domains. We also describe the functional features of the evolutionary conserved domains of membrane-bound mucins and discuss consequences of splice events.
authors.affiliation: Inserm, UMR837, Jean Pierre Aubert Research Center, Team #5 Mucins, Epithelial Differentiation and Carcinogenesis, 1 Rue Polonovski, 59045 Lille Cedex, France. nicolas.jonckheere@inserm.fr
authors.forename: Nicolas
authors.initials: N
authors.lastname: Jonckheere
authors.forename: Nicolas
authors.initials: N
authors.lastname: Skrypek
authors.forename: Frédéric
authors.initials: F
authors.lastname: Frénois
authors.forename: Isabelle
authors.initials: I
authors.lastname: Van Seuningen
mesh_terms: D000818:Animals; D005075:Biological Evolution; D006801:Humans; D009077:Mucins / Q000737:chemistry* / Q000378:metabolism*; D017434:Protein Structure, Tertiary
chemical_list: D009077:Mucins