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The organizing principle of the platelet glycoprotein Ib–IX–V complex
Author(s) -
Li R.,
Emsley J.
Publication year - 2013
Publication title -
journal of thrombosis and haemostasis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.947
H-Index - 178
eISSN - 1538-7836
pISSN - 1538-7933
DOI - 10.1111/jth.12144
Subject(s) - bernard–soulier syndrome , von willebrand factor , glycoprotein ib , platelet membrane glycoprotein , platelet glycoprotein gpib ix complex , glycoprotein , hemostasis , platelet , protein subunit , chemistry , medicine , microbiology and biotechnology , biology , biochemistry , immunology , gene
Summary The glycoprotein ( GP )Ib– IX –V complex is the platelet receptor for von Willebrand factor and many other molecules that are critically involved in hemostasis and thrombosis. The lack of functional GPI b– IX –V complexes on the platelet surface is the cause of Bernard–Soulier syndrome, a rare hereditary bleeding disorder that is also associated with macrothrombocytopenia. GPI b– IX –V contains GPI bα, GPI bβ, GPIX and GPV subunits, all of which are type I transmembrane proteins containing leucine‐rich repeat domains. Although all of the subunits were identified decades ago, not until recently did the mechanism of complex assembly begin to emerge from a systematic characterization of inter‐subunit interactions. This review summarizes the forces driving the assembly of GPI b– IX –V, discusses their implications for the pathogenesis of Bernard–Soulier syndrome, and identifies questions that remain about the structure and organization of GPI b– IX –V.