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  Recruitment of integrin ανβ3 to integrin α5β1-induced clusters enables focal adhesion maturation and cell spreading

Diaz, C., Neubauer, S., Rechenmacher, F., Kessler, H., & Missirlis, D. (2020). Recruitment of integrin ανβ3 to integrin α5β1-induced clusters enables focal adhesion maturation and cell spreading. Journal of Cell Science, 133(1): 232702, pp. 1-14. doi:10.1242/jcs.232702.

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Item Permalink: http://hdl.handle.net/21.11116/0000-0005-4F60-7 Version Permalink: http://hdl.handle.net/21.11116/0000-0005-6F27-4
Genre: Journal Article
Alternative Title : Recruitment of integrin ανbeta3 to integrin α5beta1-induced clusters enables focal adhesion maturation and cell spreading

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JCellScience_133_2020_232702.pdf (Any fulltext), 13MB
 
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 Creators:
Diaz, Carolina1, 2, Author              
Neubauer, Stefanie, Author
Rechenmacher, Florian, Author
Kessler, Horst, Author
Missirlis, Dimitris1, 2, Author              
Affiliations:
1Cellular Biophysics, Max Planck Institute for Medical Research, Max Planck Society, ou_2364731              
2Biophysical Chemistry, Institute of Physical Chemistry, University of Heidelberg, 69120 Heidelberg, Germany, ou_persistent22              

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Free keywords: fibronectin, mechanosensing, cell adhesion, endothelial cells, nano-structured substrates, hydrogels
 Abstract: The major fibronectin (FN) binding integrins α5β1 and αvβ3 exhibit cooperativity during cell adhesion, migration and mechanosensing, through mechanisms that are not yet fully resolved. Exploiting mechanically-tunable, nano-patterned substrates, and peptidomimetic ligands designed to selectively bind corresponding integrins, we report that focal adhesions (FAs) of endothelial cells assembled on integrin α5β1-selective substrates, rapidly recruit αvβ3 integrins, but not vice versa. Blocking of integrin αvβ3 hindered FA maturation and cell spreading on α5β1-selective substrates, indicating a mechanism dependent on extracellular ligand binding and highlighting the requirement of αvβ3 engagement for efficient adhesion. Recruitment of αvβ3 integrins additionally occurred on hydrogel substrates of varying mechanical properties, above a threshold stiffness supporting FA formation. Mechanistic studies revealed the need for soluble factors present in serum to allow recruitment, and excluded exogenous, or endogenous, FN as the responsible ligand for integrin αvβ3 accumulation to adhesion clusters. Our findings highlight a novel mechanism of integrin co-operation and the critical role for αvβ3 integrins in promoting cell adhesion on α5β1-selective substrates.

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Language(s): eng - English
 Dates: 2019-04-052019-11-252019-11-282020-01-02
 Publication Status: Published in print
 Pages: 14
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Degree: -

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Title: Journal of Cell Science
Source Genre: Journal
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Publ. Info: Cambridge, U.K. : Co. of Biologists
Pages: - Volume / Issue: 133 (1) Sequence Number: 232702 Start / End Page: 1 - 14 Identifier: ISSN: 0021-9533
CoNE: https://pure.mpg.de/cone/journals/resource/954925326678