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Significance Integrin inside-out activation is initiated by the α/β separation at the cytoplasmic and transmembrane domains. Such separation leads to complicated local and global conformational rearrangements of β subunit, while the conformational change of α subunit is relatively simple. It is unclear whether the global structural changes of β subunit depend on the α subunit. Using a single-chain β3 construct to mimic an extreme condition of fully separated α/β heterodimer, we show that the β3 subunit autonomously drives the membrane-dependent bent-to-extended conformational rearrangement in the absence of the α subunit. In addition, we show that the clinically important anti–HPA-1a (β3 -L33) alloantibodies perform the conformation-dependent property when interfering with the β3 integrin, which may correlate with the pathogenesis of β3 -mediated alloimmune thrombocytopenia.

Autonomous conformational regulation of β 3 integrin and the conformation-dependent property of HPA-1a alloantibodies

Autonomous conformational regulation of β ₃ integrin and the conformation-dependent property of HPA-1a alloantibodies