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Article Dans Une Revue Biochimica et Biophysica Acta (BBA) - Reviews on Cancer Année : 2012

Membrane-bound mucin modular domains: From structure to function

Résumé

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.

Dates et versions

hal-02905700 , version 1 (30-09-2020)

Identifiants

Citer

Nicolas Jonckheere, Frédéric Frénois, Isabelle van Seuningen, Nicolas Q1, Nicolas Skrypek, et al.. Membrane-bound mucin modular domains: From structure to function. Biochimica et Biophysica Acta (BBA) - Reviews on Cancer, 2012, ⟨10.1016/j.biochi.2012.11.005⟩. ⟨hal-02905700⟩

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