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Effects of the association of the α v β 8 lower legs on integrin ligand binding
Author(s) -
Song Guannan,
Luo BingHao
Publication year - 2021
Publication title -
journal of cellular biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.028
H-Index - 165
eISSN - 1097-4644
pISSN - 0730-2312
DOI - 10.1002/jcb.29912
Subject(s) - integrin , cd49c , chemistry , ligand (biochemistry) , mutant , integrin, beta 6 , biophysics , microbiology and biotechnology , binding site , cell , receptor , biochemistry , biology , gene
Many integrins transmit signals through global conformational changes. However, it is unclear whether integrin α v β 8 adopts a similar mechanism during integrin activation and signaling on the cell surface. Here, we showed that disulfide‐bonded mutants, which prevented integrin α v β 8 lower leg dissociation, bound ligands with similar level as the wild‐type protein, suggesting that α v β 8 ligand binding did not require lower leg disassociation. We further showed that the N‐glycosylation mutant at the interface between the β I and hybrid domains did not affect ligand binding, suggesting that the α v β 8 open headpiece was not present on the cell surface. We proposed that α v β 8 integrin may adopt only one state, that is, the extended conformation with a closed headpiece. Our results showed that two lower legs retained heterodimeric interfaces, and this association might be important for stabilizing integrin in the extended conformation. Therefore, α v β 8 may not transmit bidirectional signals across the plasma membrane but instead may serve as an anchoring site with high affinity and high accessibility for extracellular ligands.

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