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Wiskott–Aldrich syndrome protein is involved in αIIbβ3‐mediated cell adhesion
Author(s) -
Tsuboi Shigeru,
oyama Shigeaki,
Ochs Hans D
Publication year - 2006
Publication title -
embo reports
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 4.584
H-Index - 184
eISSN - 1469-3178
pISSN - 1469-221X
DOI - 10.1038/sj.embor.7400665
Subject(s) - wiskott–aldrich syndrome protein , platelet , wiskott–aldrich syndrome , integrin , mutant , biology , microbiology and biotechnology , cell adhesion , actin , gene , cell , genetics , immunology , actin cytoskeleton , cytoskeleton
The Wiskott–Aldrich syndrome (WAS) is an X‐chromosome‐linked immunodeficiency disorder. The most common symptom seen in WAS patients is bleeding. One of the main causes of bleeding is defective platelet aggregation. The causative gene of WAS encodes WAS protein (WASP). Here, we show that WASP binds to the calcium‐ and integrin‐binding protein (CIB) in platelets. CIB was originally identified as a protein binding to the αIIb cytoplasmic tail of platelet integrin αIIbβ3, which has a primary role in platelet aggregation. We also show that the WASP–CIB complex is important in αIIbβ3‐mediated cell adhesion, and that in patients mutant forms of WASP are expressed at reduced levels or show lower affinities for CIB than wild‐type WASP. Our results indicate that impaired complex formation between mutant WASPs and CIB reduces αIIbβ3‐mediated cell adhesion and causes defective platelet aggregation, resulting in bleeding.