Disruption of Ca2+-dependent cell-matrix adhesion enhances c-Src kinase activity, but causes dissociation of the c-Src/FAK complex and dephosphorylation of tyrosine-577 of FAK in carcinoma cells (Q40598627)

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scientific article published on February 2004

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English	Disruption of Ca2+-dependent cell-matrix adhesion enhances c-Src kinase activity, but causes dissociation of the c-Src/FAK complex and dephosphorylation of tyrosine-577 of FAK in carcinoma cells	scientific article published on February 2004

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scholarly article

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Europe PubMed Central

PubMed publication ID

21 September 2017

Disruption of Ca2+-dependent cell-matrix adhesion enhances c-Src kinase activity, but causes dissociation of the c-Src/FAK complex and dephosphorylation of tyrosine-577 of FAK in carcinoma cells (English)

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Europe PubMed Central

PubMed publication ID

21 September 2017

author name string

Eva H Lin

1

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Europe PubMed Central

PubMed publication ID

21 September 2017

Angela Y Hui

2

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Europe PubMed Central

PubMed publication ID

21 September 2017

Jalna A Meens

3

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Europe PubMed Central

PubMed publication ID

21 September 2017

Eric A Tremblay

4

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Europe PubMed Central

PubMed publication ID

21 September 2017

Erik Schaefer

5

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Europe PubMed Central

PubMed publication ID

21 September 2017

Bruce E Elliott

6

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Europe PubMed Central

PubMed publication ID

21 September 2017

language of work or name

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publication date

1 February 2004

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21 September 2017

Experimental Cell Research

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PubMed publication ID

21 September 2017

293

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Europe PubMed Central

PubMed publication ID

21 September 2017

1

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Europe PubMed Central

PubMed publication ID

21 September 2017

1-13

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Europe PubMed Central

PubMed publication ID

21 September 2017

Induction and regulation of epithelial-mesenchymal transitions

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Structure. An anthropomorphic integrin

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Molecular interactions in cell adhesion complexes

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Cellular functions regulated by Src family kinases

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Direct binding of C-terminal region of p130Cas to SH2 and SH3 domains of Src kinase

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Paxillin and focal adhesion signalling

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c-Src protein expression is increased in human breast cancer. An immunohistochemical and biochemical analysis

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Selected glimpses into the activation and function of Src kinase

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Adhesion-linked kinases in cancer; emphasis on src, focal adhesion kinase and PI 3-kinase

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Paxillin: a new vinculin-binding protein present in focal adhesions

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A new method for isolating tyrosine kinase substrates used to identify fish, an SH3 and PX domain-containing protein, and Src substrate

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Tyrosine phosphorylation of focal adhesion kinase at sites in the catalytic domain regulates kinase activity: a role for Src family kinases

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Focal adhesion kinase tyrosine-861 is a major site of phosphorylation by Src.

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Overexpression of c-Src enhances cell-matrix adhesion and cell migration in PDGF-stimulated NIH3T3 fibroblasts

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c-Src enhances the spreading of src-/- fibroblasts on fibronectin by a kinase-independent mechanism

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The catalytic activity of Src is dispensable for translocation to focal adhesions but controls the turnover of these structures during cell motility

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A mechanism for regulation of the adhesion-associated proteintyrosine kinase pp125FAK.

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7 January 2021

Inhibition of focal adhesion kinase (FAK) signaling in focal adhesions decreases cell motility and proliferation

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SRC catalytic but not scaffolding function is needed for integrin-regulated tyrosine phosphorylation, cell migration, and cell spreading

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c-Src kinase activity is required for hepatocyte growth factor-induced motility and anchorage-independent growth of mammary carcinoma cells

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Fibronectin fibrils and growth factors stimulate anchorage-independent growth of a murine mammary carcinoma

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Discovery of a novel, potent, and Src family-selective tyrosine kinase inhibitor. Study of Lck- and FynT-dependent T cell activation

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Src family kinases are required for integrin but not PDGFR signal transduction.

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Prolactin and glucocorticoid hormones synergistically induce expression of transfected rat beta-casein gene promoter constructs in a mammary epithelial cell line

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Co-operative effect of c-Src tyrosine kinase and Stat3 in activation of hepatocyte growth factor expression in mammary carcinoma cells

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Regulation of the Src protein tyrosine kinase

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Disruption of cell-substrate adhesion activates the protein tyrosine kinase pp60(c-src).

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Integrins can collaborate with growth factors for phosphorylation of receptor tyrosine kinases and MAP kinase activation: roles of integrin aggregation and occupancy of receptors

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Integrin function: molecular hierarchies of cytoskeletal and signaling molecules

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CD44 interaction with c-Src kinase promotes cortactin-mediated cytoskeleton function and hyaluronic acid-dependent ovarian tumor cell migration

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A role for epidermal growth factor receptor, c-Src and focal adhesion kinase in an in vitro model for the progression of colon cancer

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Ezrin interacts with focal adhesion kinase and induces its activation independently of cell-matrix adhesion

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v-Src induces tyrosine phosphorylation of focal adhesion kinase independently of tyrosine 397 and formation of a complex with Src

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Attenuation of adhesion-dependent signaling and cell spreading in transformed fibroblasts lacking protein tyrosine phosphatase-1B.

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Binding of the Src SH2 domain to phosphopeptides is determined by residues in both the SH2 domain and the phosphopeptides

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Three-dimensional structure of the tyrosine kinase c-Src

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Src-induced de-regulation of E-cadherin in colon cancer cells requires integrin signalling.

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Activating SRC mutation in a subset of advanced human colon cancers

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Matrix metalloproteinase stromelysin-1 triggers a cascade of molecular alterations that leads to stable epithelial-to-mesenchymal conversion and a premalignant phenotype in mammary epithelial cells

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Identifiers

10.1016/J.YEXCR.2003.09.008

1 reference

Europe PubMed Central

PubMed publication ID

21 September 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

21 September 2017

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