Article ; Online: Talin and kindlin use integrin tail allostery and direct binding to activate integrins.
Nature structural & molecular biology
2023 Volume 30, Issue 12, Page(s) 1913–1924
Abstract: Integrin affinity regulation, also termed integrin activation, is essential for metazoan life. Although talin and kindlin binding to the β-integrin cytoplasmic tail is indispensable for integrin activation, it is unknown how they achieve this function. ... ...
Abstract | Integrin affinity regulation, also termed integrin activation, is essential for metazoan life. Although talin and kindlin binding to the β-integrin cytoplasmic tail is indispensable for integrin activation, it is unknown how they achieve this function. By combining NMR, biochemistry and cell biology techniques, we found that talin and kindlin binding to the β-tail can induce a conformational change that increases talin affinity and decreases kindlin affinity toward it. We also discovered that this asymmetric affinity regulation is accompanied by a direct interaction between talin and kindlin, which promotes simultaneous binding of talin and kindlin to β-tails. Disrupting allosteric communication between the β-tail-binding sites of talin and kindlin or their direct interaction in cells severely compromised integrin functions. These data show how talin and kindlin cooperate to generate a small but critical population of ternary talin-β-integrin-kindlin complexes with high talin-integrin affinity and high dynamics. |
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MeSH term(s) | Animals ; Talin/chemistry ; Talin/metabolism ; Integrins/metabolism ; Binding Sites ; Protein Binding |
Chemical Substances | Talin ; Integrins |
Language | English |
Publishing date | 2023-12-12 |
Publishing country | United States |
Document type | Journal Article |
ZDB-ID | 2126708-X |
ISSN | 1545-9985 ; 1545-9993 |
ISSN (online) | 1545-9985 |
ISSN | 1545-9993 |
DOI | 10.1038/s41594-023-01139-9 |
Database | MEDical Literature Analysis and Retrieval System OnLINE |
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