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http://purl.uniprot.org/citations/11785963http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11785963http://www.w3.org/2000/01/rdf-schema#comment"Studies were carried out using vinculin-deficient F9 embryonic carcinoma (gamma229) cells to analyze the relationship between structure and function within the focal adhesion protein vinculin, in the context of control of cell shape, cell mechanics, and movement. Atomic force microscopy studies revealed that transfection of the head (aa 1-821) or tail (aa 811-1066) domain of vinculin, alone or together, was unable to fully reverse the decrease in cell stiffness, spreading, and lamellipodia formation caused by vinculin deficiency. In contrast, replacement with intact vinculin completely restored normal cell mechanics and spreading regardless of whether its tyrosine phosphorylation site was deleted. Constitutively active rac also only induced extension of lamellipodia when microinjected into cells that expressed intact vinculin protein. These data indicate that vinculin's ability to physically couple integrins to the cytoskeleton, to mechanically stabilize cell shape, and to support rac-dependent lamellipodia formation all appear to depend on its intact three-dimensional structure."xsd:string
http://purl.uniprot.org/citations/11785963http://purl.org/dc/terms/identifier"doi:10.1006/bbrc.2001.6243"xsd:string
http://purl.uniprot.org/citations/11785963http://purl.uniprot.org/core/author"Goldmann W.H."xsd:string
http://purl.uniprot.org/citations/11785963http://purl.uniprot.org/core/author"Ingber D.E."xsd:string
http://purl.uniprot.org/citations/11785963http://purl.uniprot.org/core/author"Ingber D.E.'"xsd:string
http://purl.uniprot.org/citations/11785963http://purl.uniprot.org/core/date"2002"xsd:gYear
http://purl.uniprot.org/citations/11785963http://purl.uniprot.org/core/name"Biochem Biophys Res Commun"xsd:string
http://purl.uniprot.org/citations/11785963http://purl.uniprot.org/core/pages"749-755"xsd:string
http://purl.uniprot.org/citations/11785963http://purl.uniprot.org/core/title"Intact vinculin protein is required for control of cell shape, cell mechanics, and rac-dependent lamellipodia formation."xsd:string
http://purl.uniprot.org/citations/11785963http://purl.uniprot.org/core/volume"290"xsd:string
http://purl.uniprot.org/citations/11785963http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/11785963
http://purl.uniprot.org/citations/11785963http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/11785963
http://purl.uniprot.org/uniprot/#_Q64727-mappedCitation-11785963http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/11785963
http://purl.uniprot.org/uniprot/#_Q9ESQ3-mappedCitation-11785963http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/11785963
http://purl.uniprot.org/uniprot/Q64727http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/11785963
http://purl.uniprot.org/uniprot/Q9ESQ3http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/11785963