About: CAS directly interacts with vinculin to control mechanosensing and focal adhesion dynamics

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An Entity of Type : http://linked.opendata.cz/ontology/domain/vavai/Vysledek, within Data Space : linked.opendata.cz associated with source document(s)

Attributes	Values
rdf:type	skos:Concept http://linked.opendata.cz/ontology/domain/vavai/Vysledek
rdfs:seeAlso	http://dx.doi.org/10.1007/s00018-013-1450-x
Description	Focal adhesions are cellular structures through which both mechanical forces and regulatory signals are transmitted. Two focal adhesion-associated proteins, Crk-associated substrate (CAS) and vinculin, were both independently shown to be crucial for the ability of cells to transmit mechanical forces and to regulate cytoskeletal tension. Here, we identify a novel, direct binding interaction between CAS and vinculin. This interaction is mediated by the CAS SRC homology 3 domain and a proline-rich sequence in the hinge region of vinculin. We show that CAS localization in focal adhesions is partially dependent on vinculin, and that CAS-vinculin coupling is required for stretch-induced activation of CAS at the Y410 phosphorylation site. Moreover, CAS-vinculin binding significantly affects the dynamics of CAS and vinculin within focal adhesions as well as the size of focal adhesions. Finally, disruption of CAS binding to vinculin reduces cell stiffness and traction force generation. Taken together, these findings strongly implicate a crucial role of CAS-vinculin interaction in mechanosensing and focal adhesion dynamics. Focal adhesions are cellular structures through which both mechanical forces and regulatory signals are transmitted. Two focal adhesion-associated proteins, Crk-associated substrate (CAS) and vinculin, were both independently shown to be crucial for the ability of cells to transmit mechanical forces and to regulate cytoskeletal tension. Here, we identify a novel, direct binding interaction between CAS and vinculin. This interaction is mediated by the CAS SRC homology 3 domain and a proline-rich sequence in the hinge region of vinculin. We show that CAS localization in focal adhesions is partially dependent on vinculin, and that CAS-vinculin coupling is required for stretch-induced activation of CAS at the Y410 phosphorylation site. Moreover, CAS-vinculin binding significantly affects the dynamics of CAS and vinculin within focal adhesions as well as the size of focal adhesions. Finally, disruption of CAS binding to vinculin reduces cell stiffness and traction force generation. Taken together, these findings strongly implicate a crucial role of CAS-vinculin interaction in mechanosensing and focal adhesion dynamics. (en)
Title	CAS directly interacts with vinculin to control mechanosensing and focal adhesion dynamics CAS directly interacts with vinculin to control mechanosensing and focal adhesion dynamics (en)
skos:prefLabel	CAS directly interacts with vinculin to control mechanosensing and focal adhesion dynamics CAS directly interacts with vinculin to control mechanosensing and focal adhesion dynamics (en)
skos:notation	RIV/00216208:11310/14:10210779!RIV15-MSM-11310___
http://linked.open...avai/riv/aktivita	I P Z
http://linked.open...avai/riv/aktivity	I, P(GC13-24851J), Z(MSM0021620858)
http://linked.open...iv/cisloPeriodika	4
http://linked.open...vai/riv/dodaniDat	2015
http://linked.open...aciTvurceVysledku	Gemperle, Jakub Brábek, Jan Rösel, Daniel Janoštiak, Radoslav Tatárová, Zuzana
http://linked.open.../riv/druhVysledku	J - Článek v odborném periodiku
http://linked.open...iv/duvernostUdaju	S - Úplné a pravdivé údaje nepodléhající ochraně podle zvláštních právních předpisů
http://linked.open...titaPredkladatele	Univerzita Karlova v Praze / Přírodovědecká fakulta
http://linked.open...dnocenehoVysledku	6255
http://linked.open...ai/riv/idVysledku	RIV/00216208:11310/14:10210779
http://linked.open...riv/jazykVysledku	eng - angličtina
http://linked.open.../riv/klicovaSlova	Traction forces; Src; Vinculin; Mechanosensing; Focal adhesions; CAS (en)
http://linked.open.../riv/klicoveSlovo	CAS Focal adhesions Mechanosensing Src Traction forces Vinculin
http://linked.open...odStatuVydavatele	CH - Švýcarská konfederace
http://linked.open...ontrolniKodProRIV	[23D6C85B6973]
http://linked.open...i/riv/nazevZdroje	Cellular and Molecular Life Sciences
http://linked.open...in/vavai/riv/obor	EB
http://linked.open...ichTvurcuVysledku	5 (xsd:int)
http://linked.open...cetTvurcuVysledku	11 (xsd:int)
http://linked.open...vavai/riv/projekt	Dissecting of BCAR1/CAS role in mechanosensing
http://linked.open...UplatneniVysledku	2014
http://linked.open...v/svazekPeriodika	71
http://linked.open...iv/tvurceVysledku	Brábek, Jan Janoštiak, Radoslav Rösel, Daniel Tatárová, Zuzana Auernheimer, Vera Dey, Tuli Fabry, Ben Gemperle, Jakub Goldmann, Wolfgang H. Lautscham, Lena A. Merkel, Rudolf
http://linked.open...ain/vavai/riv/wos	000330586500013
http://linked.open...n/vavai/riv/zamer	Signaling and cellular response mechanisms
issn	1420-682X
number of pages	18 (xsd:int)
http://bibframe.org/vocab/doi	10.1007/s00018-013-1450-x
http://localhost/t...ganizacniJednotka	11310

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