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Cell ; 187(12): 2990-3005.e17, 2024 Jun 06.
Artigo em Inglês | MEDLINE | ID: mdl-38772370

RESUMO

Integrins link the extracellular environment to the actin cytoskeleton in cell migration and adhesiveness. Rapid coordination between events outside and inside the cell is essential. Single-molecule fluorescence dynamics show that ligand binding to the bent-closed integrin conformation, which predominates on cell surfaces, is followed within milliseconds by two concerted changes, leg extension and headpiece opening, to give the high-affinity integrin conformation. The extended-closed integrin conformation is not an intermediate but can be directly accessed from the extended-open conformation and provides a pathway for ligand dissociation. In contrast to ligand, talin, which links the integrin ß-subunit cytoplasmic domain to the actin cytoskeleton, modestly stabilizes but does not induce extension or opening. Integrin activation is thus initiated by outside-in signaling and followed by inside-out signaling. Our results further imply that talin binding is insufficient for inside-out integrin activation and that tensile force transmission through the ligand-integrin-talin-actin cytoskeleton complex is required.


Assuntos
Integrinas , Talina , Animais , Humanos , Camundongos , Citoesqueleto de Actina/metabolismo , Citoesqueleto de Actina/química , Adesão Celular , Células CHO , Cricetulus , Integrinas/metabolismo , Integrinas/química , Ligantes , Ligação Proteica , Conformação Proteica , Transdução de Sinais , Imagem Individual de Molécula , Talina/metabolismo , Talina/química
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