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  Rap1 and membrane lipids cooperatively recruit talin to trigger integrin activation

Bromberger, T., Zhu, L., Klapproth, S., Qin, J., & Moser, M. (2019). Rap1 and membrane lipids cooperatively recruit talin to trigger integrin activation. JOURNAL OF CELL SCIENCE, 132(21): UNSP jcs235531. doi:10.1242/jcs.235531.

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Genre: Journal Article
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 Creators:
Bromberger, Thomas1, Author              
Zhu, Liang2, Author
Klapproth, Sarah1, Author              
Qin, Jun2, Author
Moser, Markus1, Author              
Affiliations:
1Fässler, Reinhard / Molecular Medicine, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565147              
2external, ou_persistent22              

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Free keywords: ADAPTER MOLECULE RIAM; EFFECTOR RIAM; DOMAIN; BINDING; HEAD; LOCALIZATION; CONFORMATION; ADHESION; DISTINCT; COMPLEXIntegrin; Small GTPase; Rap1; Talin; RIAM; NMR;
 Abstract: Recruitment and tethering of talin to the plasma membrane initiate the process of integrin activation. Multiple factors including the Rap1 proteins, RIAM (also known as APBB1IP) and PIP2 bind talin proteins and have been proposed to regulate these processes, but not systematically analyzed. By expressing specific talin mutants into talin-null fibroblasts, we show that binding of the talin F0 domain to Rap1 synergizes with membrane lipid binding of the talin F2 domain during talin membrane targeting and integrin activation, whereas the interaction of the talin rod with RIAM was dispensable. We also characterized a second Rap1-binding site within the talin F1 domain by detailed NMR analysis. Interestingly, while talin F1 exhibited significantly weaker Rap1-binding affinity than talin F0, expression of a talin F1 Rap1-binding mutant inhibited cell adhesion, spreading, talin recruitment and integrin activation similarly to the talin F0 Rap1-binding mutant. Moreover, the defects became significantly stronger when both Rap1-binding sites weremutated. In conclusion, our data suggest a model in which cooperative binding of Rap1 to the talin F0 and F1 domains synergizes with membrane PIP2 binding to spatiotemporally position and activate talins to regulate integrin activity.

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Language(s): eng - English
 Dates: 2019
 Publication Status: Published online
 Pages: 10
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: ISI: 000498398200012
DOI: 10.1242/jcs.235531
 Degree: -

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Title: JOURNAL OF CELL SCIENCE
Source Genre: Journal
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Publ. Info: BIDDER BUILDING, STATION RD, HISTON, CAMBRIDGE CB24 9LF, ENGLAND : COMPANY BIOLOGISTS LTD
Pages: - Volume / Issue: 132 (21) Sequence Number: UNSP jcs235531 Start / End Page: - Identifier: ISSN: 0021-9533