The adaptor protein shb binds to tyrosine 1175 in vascular endothelial growth factor (VEGF) receptor-2 and regulates VEGF-dependent cellular migration (Q28250994)

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English	The adaptor protein shb binds to tyrosine 1175 in vascular endothelial growth factor (VEGF) receptor-2 and regulates VEGF-dependent cellular migration	scientific article

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The adaptor protein shb binds to tyrosine 1175 in vascular endothelial growth factor (VEGF) receptor-2 and regulates VEGF-dependent cellular migration (English)

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Lena Claesson-Welsh

7

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Lena Claesson-Welsh

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author name string

Kristina Holmqvist

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Michael J Cross

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Charlotte Rolny

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Robert Hägerkvist

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Nader Rahimi

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Taro Matsumoto

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Michael Welsh

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publication date

21 May 2004

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Journal of Biological Chemistry

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279

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21

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22267-75

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Platelet-derived growth factor-mediated signaling through the Shb adaptor protein: effects on cytoskeletal organization

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Requirement of the Src homology 2 domain protein Shb for T cell receptor-dependent activation of the interleukin-2 gene nuclear factor for activation of T cells element in Jurkat T cells

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IL-2 receptor signaling through the Shb adapter protein in T and NK cells

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Shf, a Shb-like adapter protein, is involved in PDGF-alpha-receptor regulation of apoptosis.

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VEGF-receptor signal transduction

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Failure of blood-island formation and vasculogenesis in Flk-1-deficient mice

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The Shb adaptor protein causes Src-dependent cell spreading and activation of focal adhesion kinase in murine brain endothelial cells

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Reduced cell motility and enhanced focal adhesion contact formation in cells from FAK-deficient mice

1 reference

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Induction of tubulogenesis in telomerase-immortalized human microvascular endothelial cells by glioblastoma cells

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Stimulation through the T cell receptor leads to interactions between SHB and several signaling proteins

1 reference

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Recruitment and activation of phospholipase Cgamma1 by vascular endothelial growth factor receptor-2 are required for tubulogenesis and differentiation of endothelial cells

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Src kinase becomes preferentially associated with the VEGFR, KDR/Flk-1, following VEGF stimulation of vascular endothelial cells

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A single autophosphorylation site on KDR/Flk-1 is essential for VEGF-A-dependent activation of PLC-gamma and DNA synthesis in vascular endothelial cells

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Interactions of FLT-1 and KDR with phospholipase C gamma: identification of the phosphotyrosine binding sites

1 reference

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The Shc-related adaptor protein, Sck, forms a complex with the vascular-endothelial-growth-factor receptor KDR in transfected cells

1 reference

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Potent and specific genetic interference by double-stranded RNA in Caenorhabditis elegans

1 reference

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Targeted deficiency or cytosolic truncation of the VE-cadherin gene in mice impairs VEGF-mediated endothelial survival and angiogenesis

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Vascular endothelial growth factor stimulates tyrosine phosphorylation and recruitment to new focal adhesions of focal adhesion kinase and paxillin in endothelial cells

1 reference

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Vascular endothelial growth factor regulates focal adhesion assembly in human brain microvascular endothelial cells through activation of the focal adhesion kinase and related adhesion focal tyrosine kinase

1 reference

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Rho family proteins: coordinating cell responses

1 reference

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Induced focal adhesion kinase (FAK) expression in FAK-null cells enhances cell spreading and migration requiring both auto- and activation loop phosphorylation sites and inhibits adhesion-dependent tyrosine phosphorylation of Pyk2.

1 reference

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Focal adhesion kinase: a regulator of focal adhesion dynamics and cell movement

1 reference

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Identifiers

10.1074/JBC.M312729200

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Consolidated OpenCitations Corpus – April 2017

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OpenCitations bibliographic resource ID

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Consolidated OpenCitations Corpus – April 2017

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PubMed publication ID

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Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

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