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Talin and kindlin use integrin tail allostery and direct binding to activate integrins.
Nat. Struct. Mol. Biol. 30, 1913-1924 (2023)
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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Publication type
Article: Journal article
Document type
Scientific Article
Keywords
Structural Basis; Adhesion Measurements; Domain; Complexes; Reveals
ISSN (print) / ISBN
1545-9993
e-ISSN
1545-9985
Quellenangaben
Volume: 30,
Issue: 12,
Pages: 1913-1924
Publisher
Nature Publishing Group
Publishing Place
New York, NY
Non-patent literature
Publications
Reviewing status
Peer reviewed
Institute(s)
Institute of Structural Biology (STB)
Grants
Max Planck Society
Swiss National Science Foundation
DFG
European Research Council
Swiss National Science Foundation
DFG
European Research Council