Phosphorylation of Tyr1214 within VEGFR-2 triggers the recruitment of Nck and activation of Fyn leading to SAPK2/p38 activation and endothelial cell migration in response to VEGF (Q24302435)

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English	Phosphorylation of Tyr1214 within VEGFR-2 triggers the recruitment of Nck and activation of Fyn leading to SAPK2/p38 activation and endothelial cell migration in response to VEGF	scientific article

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Phosphorylation of Tyr1214 within VEGFR-2 triggers the recruitment of Nck and activation of Fyn leading to SAPK2/p38 activation and endothelial cell migration in response to VEGF (English)

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phosphorylation

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author name string

Laurent Lamalice

1

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François Houle

2

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Jacques Huot

3

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language of work or name

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publication date

10 November 2006

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Journal of Biological Chemistry

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281

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45

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34009-20

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Role of the Flt-1 receptor tyrosine kinase in regulating the assembly of vascular endothelium

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

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Neuropilin-1 is expressed by endothelial and tumor cells as an isoform-specific receptor for vascular endothelial growth factor

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Integrating the VEGF signals leading to actin-based motility in vascular endothelial cells.

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VEGF receptor-2 Y951 signaling and a role for the adapter molecule TSAd in tumor angiogenesis

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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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Phosphorylation of tyrosine 1214 on VEGFR2 is required for VEGF-induced activation of Cdc42 upstream of SAPK2/p38.

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Regulation of vascular endothelial growth factor receptor 2-mediated phosphorylation of focal adhesion kinase by heat shock protein 90 and Src kinase activities

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VRAP is an adaptor protein that binds KDR, a receptor for vascular endothelial cell growth factor

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

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Autophosphorylation of KDR in the kinase domain is required for maximal VEGF-stimulated kinase activity and receptor internalization

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

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Tyrosine 1213 of Flt-1 is a major binding site of Nck and SHP-2.

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Cellular functions regulated by Src family kinases

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Src kinase regulation by phosphorylation and dephosphorylation

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The SH4-Unique-SH3-SH2 domains dictate specificity in signaling that differentiate c-Yes from c-Src

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Vascular endothelial growth factor-mediated activation of p38 is dependent upon Src and RAFTK/Pyk2.

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Selective requirement for Src kinases during VEGF-induced angiogenesis and vascular permeability

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Vascular endothelial growth factor (VEGF)-driven actin-based motility is mediated by VEGFR2 and requires concerted activation of stress-activated protein kinase 2 (SAPK2/p38) and geldanamycin-sensitive phosphorylation of focal adhesion kinase

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p38 MAP kinase activation by vascular endothelial growth factor mediates actin reorganization and cell migration in human endothelial cells.

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

1 reference

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Identification of vascular endothelial growth factor receptor-1 tyrosine phosphorylation sites and binding of SH2 domain-containing molecules

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The Nck family of adapter proteins: regulators of actin cytoskeleton

1 reference

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Association of p59(fyn) with the T lymphocyte costimulatory receptor CD2. Binding of the Fyn Src homology (SH) 3 domain is regulated by the Fyn SH2 domain.

1 reference

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Signaling from integrins to Fyn to Rho family GTPases regulates morphologic differentiation of oligodendrocytes.

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Nck and Crk mediate distinct VEGF-induced signaling pathways that serve overlapping functions in focal adhesion turnover and integrin activation

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SRC-family kinase Fyn phosphorylates the cytoplasmic domain of nephrin and modulates its interaction with podocin

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Essential role of Flk-1 (VEGF receptor 2) tyrosine residue 1173 in vasculogenesis in mice

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Type I collagen limits VEGFR-2 signaling by a SHP2 protein-tyrosine phosphatase-dependent mechanism 1.

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Vascular endothelial growth factor-induced endothelial cell proliferation is regulated by interaction between VEGFR-2, SH-PTP1 and eNOS.

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The vascular endothelial growth factor receptor KDR activates multiple signal transduction pathways in porcine aortic endothelial cells

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VEGF activates protein kinase C-dependent, but Ras-independent Raf-MEK-MAP kinase pathway for DNA synthesis in primary endothelial cells

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Fyn kinase acts upstream of Shp2 and p38 mitogen-activated protein kinase to promote chemotaxis of mast cells towards stem cell factor

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Biology of the p21-activated kinases

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Cdc42/Rac1-mediated activation primes PAK2 for superactivation by tyrosine phosphorylation

1 reference

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Oxidative stress-induced actin reorganization mediated by the p38 mitogen-activated protein kinase/heat shock protein 27 pathway in vascular endothelial cells

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7 January 2021

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10.1074/JBC.M603928200

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