Recruitment of integrin α ν β 3 to integrin α 5 β 1 -induced clusters enables focal adhesion maturation and cell spreading

Autores
Diaz, Carolina; Neubauer, Stefanie; Rechenmacher, Florian; Kessler, Horst; Missirlis, Dimitris
Año de publicación
2019
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
The major fibronectin (FN)-binding α5β1 and αvβ3 integrins 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 α5β1 integrin-selective substrates rapidly recruit αvβ3 integrins, but not vice versa. Blocking of αvβ3 integrin hindered FA maturation and cell spreading on α5β1 integrin-selective substrates, indicating a mechanism dependent on extracellular ligand binding and highlighting the requirement of αvβ3 integrin engagement for efficient adhesion. Recruitment of αvβ3 integrins additionally occurred on hydrogel substrates of varying mechanical properties, above a threshold stiffness that supports FA formation. Mechanistic studies revealed the need for soluble factors present in serum to allow recruitment, and excluded exogenous, or endogenous, FN as the ligand responsible for αvβ3 integrin accumulation to adhesion clusters. Our findings highlight a novel mechanism of integrin cooperation and a critical role for αvβ3 integrins in promoting cell adhesion on α5β1 integrin-selective substrates.
Fil: Diaz, Carolina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Fisicoquímicas Teóricas y Aplicadas. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Instituto de Investigaciones Fisicoquímicas Teóricas y Aplicadas; Argentina. Max Planck Institute for Medical Research; Alemania
Fil: Neubauer, Stefanie. Technische Universitat Munchen. Fakultat Fur Chemie; Alemania
Fil: Rechenmacher, Florian. Technische Universitat Munchen. Fakultat Fur Chemie; Alemania
Fil: Kessler, Horst. Technische Universitat Munchen. Fakultat Fur Chemie; Alemania
Fil: Missirlis, Dimitris. Max Planck Institute for Medical Research; Alemania. Ruprecht Karls Universitat Heidelberg.; Alemania
Materia
FIBRONECTIN
MECHANOSENSING
CELL ADHESION
ENDOTHELIAL CELLS
NANO-STRUCTURED SUBSTRATES
HYDROGELS
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/118650
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/118650
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Recruitment of integrin α ν β 3 to integrin α 5 β 1 -induced clusters enables focal adhesion maturation and cell spreadingDiaz, CarolinaNeubauer, StefanieRechenmacher, FlorianKessler, HorstMissirlis, DimitrisFIBRONECTINMECHANOSENSINGCELL ADHESIONENDOTHELIAL CELLSNANO-STRUCTURED SUBSTRATESHYDROGELShttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1The major fibronectin (FN)-binding α5β1 and αvβ3 integrins 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 α5β1 integrin-selective substrates rapidly recruit αvβ3 integrins, but not vice versa. Blocking of αvβ3 integrin hindered FA maturation and cell spreading on α5β1 integrin-selective substrates, indicating a mechanism dependent on extracellular ligand binding and highlighting the requirement of αvβ3 integrin engagement for efficient adhesion. Recruitment of αvβ3 integrins additionally occurred on hydrogel substrates of varying mechanical properties, above a threshold stiffness that supports FA formation. Mechanistic studies revealed the need for soluble factors present in serum to allow recruitment, and excluded exogenous, or endogenous, FN as the ligand responsible for αvβ3 integrin accumulation to adhesion clusters. Our findings highlight a novel mechanism of integrin cooperation and a critical role for αvβ3 integrins in promoting cell adhesion on α5β1 integrin-selective substrates.Fil: Diaz, Carolina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Fisicoquímicas Teóricas y Aplicadas. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Instituto de Investigaciones Fisicoquímicas Teóricas y Aplicadas; Argentina. Max Planck Institute for Medical Research; AlemaniaFil: Neubauer, Stefanie. Technische Universitat Munchen. Fakultat Fur Chemie; AlemaniaFil: Rechenmacher, Florian. Technische Universitat Munchen. Fakultat Fur Chemie; AlemaniaFil: Kessler, Horst. Technische Universitat Munchen. Fakultat Fur Chemie; AlemaniaFil: Missirlis, Dimitris. Max Planck Institute for Medical Research; Alemania. Ruprecht Karls Universitat Heidelberg.; AlemaniaCompany of Biologists2019-11info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/118650Diaz, Carolina; Neubauer, Stefanie; Rechenmacher, Florian; Kessler, Horst; Missirlis, Dimitris; Recruitment of integrin α ν β 3 to integrin α 5 β 1 -induced clusters enables focal adhesion maturation and cell spreading; Company of Biologists; Journal of Cell Science; 133; 11-2019; 1-140021-9533CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/http://jcs.biologists.org/lookup/doi/10.1242/jcs.232702info:eu-repo/semantics/altIdentifier/doi/10.1242/jcs.232702info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-22T11:07:34Zoai:ri.conicet.gov.ar:11336/118650instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-10-22 11:07:34.779CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Recruitment of integrin α ν β 3 to integrin α 5 β 1 -induced clusters enables focal adhesion maturation and cell spreading
title Recruitment of integrin α ν β 3 to integrin α 5 β 1 -induced clusters enables focal adhesion maturation and cell spreading
spellingShingle Recruitment of integrin α ν β 3 to integrin α 5 β 1 -induced clusters enables focal adhesion maturation and cell spreading
Diaz, Carolina
FIBRONECTIN
MECHANOSENSING
CELL ADHESION
ENDOTHELIAL CELLS
NANO-STRUCTURED SUBSTRATES
HYDROGELS
title_short Recruitment of integrin α ν β 3 to integrin α 5 β 1 -induced clusters enables focal adhesion maturation and cell spreading
title_full Recruitment of integrin α ν β 3 to integrin α 5 β 1 -induced clusters enables focal adhesion maturation and cell spreading
title_fullStr Recruitment of integrin α ν β 3 to integrin α 5 β 1 -induced clusters enables focal adhesion maturation and cell spreading
title_full_unstemmed Recruitment of integrin α ν β 3 to integrin α 5 β 1 -induced clusters enables focal adhesion maturation and cell spreading
title_sort Recruitment of integrin α ν β 3 to integrin α 5 β 1 -induced clusters enables focal adhesion maturation and cell spreading
dc.creator.none.fl_str_mv Diaz, Carolina
Neubauer, Stefanie
Rechenmacher, Florian
Kessler, Horst
Missirlis, Dimitris
author Diaz, Carolina
author_facet Diaz, Carolina
Neubauer, Stefanie
Rechenmacher, Florian
Kessler, Horst
Missirlis, Dimitris
author_role author
author2 Neubauer, Stefanie
Rechenmacher, Florian
Kessler, Horst
Missirlis, Dimitris
author2_role author
author
author
author
dc.subject.none.fl_str_mv FIBRONECTIN
MECHANOSENSING
CELL ADHESION
ENDOTHELIAL CELLS
NANO-STRUCTURED SUBSTRATES
HYDROGELS
topic FIBRONECTIN
MECHANOSENSING
CELL ADHESION
ENDOTHELIAL CELLS
NANO-STRUCTURED SUBSTRATES
HYDROGELS
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv The major fibronectin (FN)-binding α5β1 and αvβ3 integrins 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 α5β1 integrin-selective substrates rapidly recruit αvβ3 integrins, but not vice versa. Blocking of αvβ3 integrin hindered FA maturation and cell spreading on α5β1 integrin-selective substrates, indicating a mechanism dependent on extracellular ligand binding and highlighting the requirement of αvβ3 integrin engagement for efficient adhesion. Recruitment of αvβ3 integrins additionally occurred on hydrogel substrates of varying mechanical properties, above a threshold stiffness that supports FA formation. Mechanistic studies revealed the need for soluble factors present in serum to allow recruitment, and excluded exogenous, or endogenous, FN as the ligand responsible for αvβ3 integrin accumulation to adhesion clusters. Our findings highlight a novel mechanism of integrin cooperation and a critical role for αvβ3 integrins in promoting cell adhesion on α5β1 integrin-selective substrates.
Fil: Diaz, Carolina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Fisicoquímicas Teóricas y Aplicadas. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Instituto de Investigaciones Fisicoquímicas Teóricas y Aplicadas; Argentina. Max Planck Institute for Medical Research; Alemania
Fil: Neubauer, Stefanie. Technische Universitat Munchen. Fakultat Fur Chemie; Alemania
Fil: Rechenmacher, Florian. Technische Universitat Munchen. Fakultat Fur Chemie; Alemania
Fil: Kessler, Horst. Technische Universitat Munchen. Fakultat Fur Chemie; Alemania
Fil: Missirlis, Dimitris. Max Planck Institute for Medical Research; Alemania. Ruprecht Karls Universitat Heidelberg.; Alemania
description The major fibronectin (FN)-binding α5β1 and αvβ3 integrins 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 α5β1 integrin-selective substrates rapidly recruit αvβ3 integrins, but not vice versa. Blocking of αvβ3 integrin hindered FA maturation and cell spreading on α5β1 integrin-selective substrates, indicating a mechanism dependent on extracellular ligand binding and highlighting the requirement of αvβ3 integrin engagement for efficient adhesion. Recruitment of αvβ3 integrins additionally occurred on hydrogel substrates of varying mechanical properties, above a threshold stiffness that supports FA formation. Mechanistic studies revealed the need for soluble factors present in serum to allow recruitment, and excluded exogenous, or endogenous, FN as the ligand responsible for αvβ3 integrin accumulation to adhesion clusters. Our findings highlight a novel mechanism of integrin cooperation and a critical role for αvβ3 integrins in promoting cell adhesion on α5β1 integrin-selective substrates.
publishDate 2019
dc.date.none.fl_str_mv 2019-11
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/118650
Diaz, Carolina; Neubauer, Stefanie; Rechenmacher, Florian; Kessler, Horst; Missirlis, Dimitris; Recruitment of integrin α ν β 3 to integrin α 5 β 1 -induced clusters enables focal adhesion maturation and cell spreading; Company of Biologists; Journal of Cell Science; 133; 11-2019; 1-14
0021-9533
CONICET Digital
CONICET
url http://hdl.handle.net/11336/118650
identifier_str_mv Diaz, Carolina; Neubauer, Stefanie; Rechenmacher, Florian; Kessler, Horst; Missirlis, Dimitris; Recruitment of integrin α ν β 3 to integrin α 5 β 1 -induced clusters enables focal adhesion maturation and cell spreading; Company of Biologists; Journal of Cell Science; 133; 11-2019; 1-14
0021-9533
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/http://jcs.biologists.org/lookup/doi/10.1242/jcs.232702
info:eu-repo/semantics/altIdentifier/doi/10.1242/jcs.232702
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv Company of Biologists
publisher.none.fl_str_mv Company of Biologists
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
_version_ 1846781392512352256
score 12.982451

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