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- W4288902593 abstract "Abstract Insulin-like growth factors (IGFs) have pleiotropic roles in embryonic and postnatal growth and differentiation. Most serum IGFs are bound in a ternary complex with IGF-binding protein 3 (IGFBP3) and acid-labile subunit (ALS), extending the serum half-life of IGFs and regulating their availability. Here, we report cryo-EM structure of the human IGF1/IGFBP3/ALS ternary complex, revealing the detailed architecture of a parachute-like ternary complex and crucial determinants for their sequential and specific assembly. In vitro biochemical studies show that proteolysis at the central linker domain of IGFBP3 induces release of its C-terminal domain rather than IGF1 release from the ternary complex, yielding an intermediate complex that enhances IGF1 bioavailability. Our results provide mechanistic insight into IGF/IGFBP3/ALS ternary complex assembly and its disassembly upon proteolysis for IGF bioavailability, suggesting a structural basis for human diseases associated with IGF1 and IGFALS gene mutations such as complete ALS deficiency (ACLSD) and IGF1 deficiency." @default.
- W4288902593 created "2022-07-31" @default.
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- W4288902593 date "2022-07-30" @default.
- W4288902593 modified "2023-10-09" @default.
- W4288902593 title "Structural basis for assembly and disassembly of the IGF/IGFBP/ALS ternary complex" @default.
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- W4288902593 doi "https://doi.org/10.1038/s41467-022-32214-2" @default.
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