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  alpha v-Class integrin binding to fibronectin is solely mediated by RGD and unaffected by an RGE mutation

Benito-Jardon, M., Strohmeyer, N., Ortega-Sanchis, S., Bharadwaj, M., Moser, M., Mueller, D. J., et al. (2020). alpha v-Class integrin binding to fibronectin is solely mediated by RGD and unaffected by an RGE mutation. The Journal of Cell Biology, 219(12): e202004198. doi:10.1083/jcb.202004198.

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 Creators:
Benito-Jardon, Maria1, Author
Strohmeyer, Nico1, Author
Ortega-Sanchis, Sheila1, Author
Bharadwaj, Mitasha1, Author
Moser, Markus2, Author              
Mueller, Daniel J.1, Author
Fässler, Reinhard2, Author              
Costell, Mercedes1, Author
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1external, ou_persistent22              
2Fässler, Reinhard / Molecular Medicine, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565147              

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Free keywords: CELL-ADHESION; FOCAL ADHESION; ALPHA-5-BETA-1 INTEGRINS; ALPHA-4-BETA-1 INTEGRIN; HEPARAN-SULFATE; MIGRATION; RECEPTOR; DOMAIN; FIBRILLOGENESIS; POLYMERIZATIONCell Biology;
 Abstract: Fibronectin (FN) is an essential glycoprotein of the extracellular matrix; binds integrins, syndecans, collagens, and growth factors; and is assembled by cells into complex fibrillar networks. The RGD motif in FN facilitates cell binding- and fibrillogenesis through binding to alpha 5 beta 1 and alpha v-class integrins. However, whether RGD is the sole binding site for alpha v-class integrins is unclear. Most notably, substituting aspartate with glutamate (RGE) was shown to eliminate integrin binding in vitro, while mouse genetics revealed that FNRGE preserves alpha v-class integrin binding and fibrillogenesis. To address this conflict, we employed single-cell force spectroscopy, engineered cells, and RGD motif-deficient mice (Fn1(Delta RGD/Delta RGD)) to search for additional alpha v-class integrin-binding sites. Our results demonstrate that alpha 5 beta 1 and alpha v-class integrins solely recognize the FN-RGD motif and that av-class, but not alpha 5 beta 1, integrins retain FN-RGE binding. Furthermore, Fn1(Delta RGD/Delta RGD) tissues and cells assemble abnormal and dysfunctional FNARGD fibrils in a syndecan-dependent manner. Our data highlight the central role of FN Delta RGD and the functionality of FN-RGE for alpha v-class integrins.

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Language(s): eng - English
 Dates: 2020
 Publication Status: Published online
 Pages: 23
 Publishing info: -
 Table of Contents: This article has been corrected Correction: αv-Class integrin binding to fibronectin is solely mediated by RGD and unaffected by an RGE mutation
 Rev. Type: -
 Identifiers: ISI: 000607622500007
DOI: 10.1083/jcb.202004198
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Grant ID : 810104
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Funding organization : European Research Council

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Title: The Journal of Cell Biology
  Other : JBC
Source Genre: Journal
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Publ. Info: New York, NY : Rockefeller Institute Press
Pages: - Volume / Issue: 219 (12) Sequence Number: e202004198 Start / End Page: - Identifier: ISSN: 0021-9525
CoNE: https://pure.mpg.de/cone/journals/resource/991042742946024_2