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November 30, 2012

Volume 287Issue 49p40838-41568
Open Access
On The Cover: Schematic representation of the DAP(dystrophin-associated protein) complex and its interacting proteins at blood-brain barrier. Specific dystrophin isoforms can bind actin cytoskeleton and also anchor the dystroglycan subcomplex, which interacts with laminin and agrin in the basement membrane whereas neurexins have been found in endothelia. The dystrobrevin-syntrophin subcomplex is involved in anchoring the DAP at the endfoot. Moreover, closely apposed to the abluminal endothelial surface reside Kir4.1 and aquaporin-4 channels, the latter arranged in supramolecular orthogonal arrays of particles. Moreover, α-dystrobrevin (α-DB) is coupled to a number of specific binding partners with diverse functions: dysbindin and Slo-1 have been localized to glial endfeet. For details see the article by Lien et al., pages 41374–41385....
On The Cover: Schematic representation of the DAP(dystrophin-associated protein) complex and its interacting proteins at blood-brain barrier. Specific dystrophin isoforms can bind actin cytoskeleton and also anchor the dystroglycan subcomplex, which interacts with laminin and agrin in the basement membrane whereas neurexins have been found in endothelia. The dystrobrevin-syntrophin subcomplex is involved in anchoring the DAP at the endfoot. Moreover, closely apposed to the abluminal endothelial surface reside Kir4.1 and aquaporin-4 channels, the latter arranged in supramolecular orthogonal arrays of particles. Moreover, α-dystrobrevin (α-DB) is coupled to a number of specific binding partners with diverse functions: dysbindin and Slo-1 have been localized to glial endfeet. For details see the article by Lien et al., pages 41374–41385.

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