Publikation: v-Src SH3-enhanced Interaction with Focal Adhesion Kinase at Beta1 Integrin-containing Invadopodia Promotes Cell Invasion
Dateien
Datum
Autor:innen
Herausgeber:innen
ISSN der Zeitschrift
Electronic ISSN
ISBN
Bibliografische Daten
Verlag
Schriftenreihe
Auflagebezeichnung
URI (zitierfähiger Link)
Internationale Patentnummer
Link zur Lizenz
Angaben zur Forschungsförderung
Projekt
Open Access-Veröffentlichung
Sammlungen
Core Facility der Universität Konstanz
Titel in einer weiteren Sprache
Publikationstyp
Publikationsstatus
Erschienen in
Zusammenfassung
In viral Src (v-Src) transformed cells, focal adhesion kinase (FAK) associates in a stable signaling complex with v-Src that is mediated by combined v-Src SH2 and gain-of-function v-Src SH3 domain binding to FAK. Here, we assess the significance of the Arg-95 to Trp gain-of-function mutation in the v-Src SH3 domain through comparisons of Src-/- fibroblasts transformed with either Prague C v-Src or a point-mutant (v-Src-RT) containing a normal (Arg-95) SH3 domain. Both v-Src isoforms exhibited equivalent kinase activity, enhanced Src-/- cell motility, and stimulated cell growth in both low serum and soft agar. Notably, the stability of a v-Src-FAK signaling complex and FAK phosphorylation at Tyr-861 and Tyr-925 were reduced in v-Src-RT compared to v-Src-transformed cells. Significantly, v-Src but not v-Src-RT promoted Src-/- cell invasion through a reconstituted Matrigel basement membrane barrier and v-Src co-localized with FAK and ß1 integrin at invadopodia. In contrast, v-Src-RT exhibited a partial peri-nuclear and focal contact distribution in Src-/- cells. Adenoviral-mediated FAK overexpression promoted the recruitment of v-Src-RT to invadopodia, facilitated the formation of a v-Src-RT-FAK signaling complex, and reversed the v-Src-RT invasion deficit. Adenoviral-mediated dominant-negative inhibition of FAK blocked v-Src-stimulated cell invasion. These studies establish that gain-of-function v-Src SH3 targeting interactions with FAK at ß1 integrin-containing invadopodia act to stabilize a v-Src-FAK signaling complex promoting cell invasion.
Zusammenfassung in einer weiteren Sprache
Fachgebiet (DDC)
Schlagwörter
Konferenz
Rezension
Zitieren
ISO 690
HAUCK, Christof R., Datsun A. HSIA, Du ko ILIĆ, David D. SCHLAEPFER, 2002. v-Src SH3-enhanced Interaction with Focal Adhesion Kinase at Beta1 Integrin-containing Invadopodia Promotes Cell Invasion. In: Journal of Biological Chemistry. 2002, 277(15), pp. 12487-12490BibTex
@article{Hauck2002SH3en-6655, year={2002}, title={v-Src SH3-enhanced Interaction with Focal Adhesion Kinase at Beta1 Integrin-containing Invadopodia Promotes Cell Invasion}, number={15}, volume={277}, journal={Journal of Biological Chemistry}, pages={12487--12490}, author={Hauck, Christof R. and Hsia, Datsun A. and Ilić, Du ko and Schlaepfer, David D.} }
RDF
<rdf:RDF xmlns:dcterms="http://purl.org/dc/terms/" xmlns:dc="http://purl.org/dc/elements/1.1/" xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#" xmlns:bibo="http://purl.org/ontology/bibo/" xmlns:dspace="http://digital-repositories.org/ontologies/dspace/0.1.0#" xmlns:foaf="http://xmlns.com/foaf/0.1/" xmlns:void="http://rdfs.org/ns/void#" xmlns:xsd="http://www.w3.org/2001/XMLSchema#" > <rdf:Description rdf:about="https://kops.uni-konstanz.de/server/rdf/resource/123456789/6655"> <void:sparqlEndpoint rdf:resource="http://localhost/fuseki/dspace/sparql"/> <dc:language>eng</dc:language> <foaf:homepage rdf:resource="http://localhost:8080/"/> <dspace:hasBitstream rdf:resource="https://kops.uni-konstanz.de/bitstream/123456789/6655/1/v_Src_SH3_enhanced_Interaction.pdf"/> <bibo:uri rdf:resource="http://kops.uni-konstanz.de/handle/123456789/6655"/> <dcterms:isPartOf rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/28"/> <dcterms:bibliographicCitation>First publ. in: Journal of Biological Chemistry 277 (2002), 15, pp. 12487 12490</dcterms:bibliographicCitation> <dc:contributor>Schlaepfer, David D.</dc:contributor> <dcterms:title>v-Src SH3-enhanced Interaction with Focal Adhesion Kinase at Beta1 Integrin-containing Invadopodia Promotes Cell Invasion</dcterms:title> <dcterms:hasPart rdf:resource="https://kops.uni-konstanz.de/bitstream/123456789/6655/1/v_Src_SH3_enhanced_Interaction.pdf"/> <dc:creator>Ilić, Du ko</dc:creator> <dc:creator>Hauck, Christof R.</dc:creator> <dcterms:issued>2002</dcterms:issued> <dcterms:abstract xml:lang="eng">In viral Src (v-Src) transformed cells, focal adhesion kinase (FAK) associates in a stable signaling complex with v-Src that is mediated by combined v-Src SH2 and gain-of-function v-Src SH3 domain binding to FAK. Here, we assess the significance of the Arg-95 to Trp gain-of-function mutation in the v-Src SH3 domain through comparisons of Src-/- fibroblasts transformed with either Prague C v-Src or a point-mutant (v-Src-RT) containing a normal (Arg-95) SH3 domain. Both v-Src isoforms exhibited equivalent kinase activity, enhanced Src-/- cell motility, and stimulated cell growth in both low serum and soft agar. Notably, the stability of a v-Src-FAK signaling complex and FAK phosphorylation at Tyr-861 and Tyr-925 were reduced in v-Src-RT compared to v-Src-transformed cells. Significantly, v-Src but not v-Src-RT promoted Src-/- cell invasion through a reconstituted Matrigel basement membrane barrier and v-Src co-localized with FAK and ß1 integrin at invadopodia. In contrast, v-Src-RT exhibited a partial peri-nuclear and focal contact distribution in Src-/- cells. Adenoviral-mediated FAK overexpression promoted the recruitment of v-Src-RT to invadopodia, facilitated the formation of a v-Src-RT-FAK signaling complex, and reversed the v-Src-RT invasion deficit. Adenoviral-mediated dominant-negative inhibition of FAK blocked v-Src-stimulated cell invasion. These studies establish that gain-of-function v-Src SH3 targeting interactions with FAK at ß1 integrin-containing invadopodia act to stabilize a v-Src-FAK signaling complex promoting cell invasion.</dcterms:abstract> <dc:contributor>Hauck, Christof R.</dc:contributor> <dc:contributor>Ilić, Du ko</dc:contributor> <dc:format>application/pdf</dc:format> <dc:rights>Attribution-NonCommercial-NoDerivs 2.0 Generic</dc:rights> <dc:creator>Schlaepfer, David D.</dc:creator> <dspace:isPartOfCollection rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/28"/> <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-03-24T17:28:06Z</dc:date> <dc:creator>Hsia, Datsun A.</dc:creator> <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-03-24T17:28:06Z</dcterms:available> <dc:contributor>Hsia, Datsun A.</dc:contributor> <dcterms:rights rdf:resource="http://creativecommons.org/licenses/by-nc-nd/2.0/"/> </rdf:Description> </rdf:RDF>