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- W2068365812 abstract "Integrin-mediated adhesion promotes cell survival in vitro, whereas integrin antagonists induce apoptosis of adherent cells in vivo. Here, we demonstrate that cells adherent within a three-dimensional extracellular matrix undergo apoptosis due to expression of unligated integrins, the β subunit cytoplasmic domain, or its membrane proximal sequence KLLITIHDRKEF. Integrin-mediated death requires initiator, but not stress, caspase activity and is distinct from anoikis, which is caused by the loss of adhesion per se. Surprisingly, unligated integrin or β integrin tails recruit caspase-8 to the membrane, where it becomes activated in a death receptor–independent manner. Integrin ligation disrupts this integrin–caspase containing complex and increases survival, revealing an unexpected role for integrins in the regulation of apoptosis and tissue remodeling." @default.
- W2068365812 created "2016-06-24" @default.
- W2068365812 creator A5056499527 @default.
- W2068365812 creator A5057799963 @default.
- W2068365812 creator A5058566347 @default.
- W2068365812 creator A5089796560 @default.
- W2068365812 creator A5091420701 @default.
- W2068365812 date "2001-10-29" @default.
- W2068365812 modified "2023-10-16" @default.
- W2068365812 title "Apoptosis of adherent cells by recruitment of caspase-8 to unligated integrins" @default.
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- W2068365812 doi "https://doi.org/10.1083/jcb.200106070" @default.
- W2068365812 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2150834" @default.
- W2068365812 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/11684710" @default.
- W2068365812 hasPublicationYear "2001" @default.
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