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  Structure of Rap1b bound to talin reveals a pathway for triggering integrin activation

Zhu, L., Yang, J., Bromberger, T., Holly, A., Lu, F., Liu, H., et al. (2017). Structure of Rap1b bound to talin reveals a pathway for triggering integrin activation. Nature Communications, 1744 (2017). doi:10.1038/s41467-017-01822-8.

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 Creators:
Zhu, Liang1, Author
Yang, Jun1, Author
Bromberger, Thomas2, Author              
Holly, A.1, Author
Lu, F.1, Author
Liu, H.1, Author
Sun, Kevin1, Author
Klapproth, Sarah2, Author              
Hirbawi, J.1, Author
Byzova, T. V.1, Author
Plow, E. F.1, Author
Moser, Markus2, Author              
Qin, Jun1, Author
Affiliations:
1External Organizations, ou_persistent22              
2Fässler, Reinhard / Molecular Medicine, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565147              

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 Abstract: Activation of transmembrane receptor integrin by talin is essential for inducing cell adhesion. However, the pathway that recruits talin to the membrane, which critically controls talin’s action, remains elusive. Membrane-anchored mammalian small GTPase Rap1 is known to bind talin-F0 domain but the binding was shown to be weak and thus hardly studied. Here we show structurally that talin-F0 binds to human Rap1b like canonical Rap1 effectors despite little sequence homology, and disruption of the binding strongly impairs integrin activation, cell adhesion, and cell spreading. Furthermore, while being weak in conventional binary binding conditions, the Rap1b/talin interaction becomes strong upon attachment of activated Rap1b to vesicular membranes that mimic the agonist-induced microenvironment. These data identify a crucial Rap1-mediated membrane-targeting mechanism for talin to activate integrin. They further broadly caution the analyses of weak protein–protein interactions that may be pivotal for function but neglected in the absence of specific cellular microenvironments.

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 Dates: 2017-11-23
 Publication Status: Published online
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 Identifiers: DOI: 10.1038/s41467-017-01822-8
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Title: Nature Communications
  Abbreviation : Nat. Commun.
Source Genre: Journal
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Publ. Info: London : Nature Publishing Group
Pages: - Volume / Issue: - Sequence Number: 1744 (2017) Start / End Page: - Identifier: ISSN: 2041-1723
CoNE: https://pure.mpg.de/cone/journals/resource/2041-1723