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Membrane-bound mucin modular domains: from structure to function.

Nicolas Jonckheere 1, * Nicolas Skrypek 1 Frédéric Frénois 1 Isabelle van Seuningen 1 
* Corresponding author
1 Inserm UMR837 Team 5
CHRU Lille - Centre Hospitalier Régional Universitaire [Lille], JPArc - Centre de Recherche Jean-Pierre AUBERT Neurosciences et Cancer - U1172 Inserm - U837
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.
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Submitted on : Thursday, April 4, 2013 - 2:26:49 PM
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Nicolas Jonckheere, Nicolas Skrypek, Frédéric Frénois, Isabelle van Seuningen. Membrane-bound mucin modular domains: from structure to function.. Biochimie, Elsevier, 2013, 95 (6), pp.1077-86. ⟨10.1016/j.biochi.2012.11.005⟩. ⟨inserm-00807818⟩



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