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- W2077277541 abstract "Adhesion to extracellular ligands through integrins regulates cell shape, migration, growth, and survival. How integrins transmit signals in the outside-to-in direction remains unknown. Whereas in resting integrins the α and β subunit transmembrane domains are associated, ligand binding promotes dissociation and separation of these domains. Here we address whether such separation is required for outside-in signaling. By introduction of an intersubunit disulfide bond, we generated mutant integrin αIIbβ3 with blocked transmembrane separation that binds ligand, mediates adhesion, adopts an extended conformation after ligand binding, and forms antibody-induced macroclusters on the cell surface similarly to wild type. However, the mutant integrin exhibits a profound defect in adhesion-induced outside-in signaling as measured by cell spreading, actin stress-fiber and focal adhesion formation, and focal adhesion kinase activation. This defect was rescued by reduction of the disulfide bond. Our results demonstrate that the separation of transmembrane domains is required for integrin outside-in signal transduction." @default.
- W2077277541 created "2016-06-24" @default.
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- W2077277541 creator A5062947234 @default.
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- W2077277541 date "2007-10-01" @default.
- W2077277541 modified "2023-10-18" @default.
- W2077277541 title "Requirement of α and β subunit transmembrane helix separation for integrin outside-in signaling" @default.
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- W2077277541 doi "https://doi.org/10.1182/blood-2007-03-080077" @default.
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