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IGF1 Binding to Integrin α6β4 Leads to Binding of the Calx-β Domain to Non-Catalytic (Allosteric) Site of IGF1R Kinase and Enhances Cell Survival

2026-04-20

Abstract excerpt

Previous studies showed that IGF1 binds to α6β4 and induces α6β4-IGF1-IGF1R complex, which leads to the IGF1R kinase activation. An IGF1 mutant defective in integrin binding was defective in signaling and ternary complex formation, and acted as an antagonist, although the mutant still bound to IGF1R, suggesting that IGF1 binding to α6β4 plays a critical role in IGF1R activation. β4 has a unique long tail (>1000...

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Literature Corpus work
56271096-11bc-5f4b-9af7-1e6033378e76
DOI
10.20944/preprints202604.1283.v1
Open publication

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IGF1 Binding to Integrin α6β4 Leads to Binding of the Calx-β Domain to Non-Catalytic (Allosteric) Site of IGF1R Kinase and Enhances Cell SurvivalDOI 10.20944/preprints202604.1283.v1
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