The interplay between Src and integrins in normal and tumor biology. - Wikidata - awgldk - TriplyDB

The interplay between Src and integrins in normal and tumor biology.

The interplay between Src and integrins in normal and tumor biology.

http://www.wikidata.org/entity/Q35920891

about

Rac1 and Rac3 isoform activation is involved in the invasive and metastatic phenotype of human breast cancer cells Tyrosine phosphorylation of the orphan receptor ESDN/DCBLD2 serves as a scaffold for the signaling adaptor CrkL CAP interacts with cytoskeletal proteins and regulates adhesion-mediated ERK activation and motility Integrative genomic and proteomic analyses identify targets for Lkb1-deficient metastatic lung tumors Increased cytoplasmic level of migfilin is associated with higher grades of human leiomyosarcoma CUB domain-containing protein 1 is a novel regulator of anoikis resistance in lung adenocarcinoma Heparan Sulfate Proteoglycans May Promote or Inhibit Cancer Progression by Interacting with Integrins and Affecting Cell Migration The molecular effect of metastasis suppressors on Src signaling and tumorigenesis: new therapeutic targets Role of adhesion receptor trafficking in 3D cell migration SRC: marker or actor in prostate cancer aggressiveness Targeting Src family kinases in anti-cancer therapies: turning promise into triumph Regulation of Xenopus gastrulation by ErbB signaling.Apc mutation enhances PyMT-induced mammary tumorigenesis The spatiotemporal pattern of Src activation at lipid rafts revealed by diffusion-corrected FRET imaging Leptin enhances the potency of circulating angiogenic cells via src kinase and integrin (alpha)vbeta5: implications for angiogenesis in human obesity Spatiotemporal regulation of Src and its substrates at invadosomes The integrin antagonist cilengitide activates alphaVbeta3, disrupts VE-cadherin localization at cell junctions and enhances permeability in endothelial cells Laminin-332-beta1 integrin interactions negatively regulate invadopodia Theoretical Insights Reveal Novel Motions in Csk's SH3 Domain That Control Kinase Activation.Kindlin-2 tyrosine phosphorylation and interaction with Src serve as a regulatable switch in the integrin outside-in signaling circuit.Engineered kinase activation reveals unique morphodynamic phenotypes and associated trafficking for Src family isoforms.Distal loop flexibility of a regulatory domain modulates dynamics and activity of C-terminal SRC kinase (csk)The evolutionarily conserved arrangement of domains in SRC family kinases is important for substrate recognition.Crystal structure of the FERM domain of focal adhesion kinase.Src and FAK kinases cooperate to phosphorylate paxillin kinase linker, stimulate its focal adhesion localization, and regulate cell spreading and protrusiveness.SPARC mediates Src-induced disruption of actin cytoskeleton via inactivation of small GTPases Rho-Rac-Cdc42 Integrins and cadherins join forces to form adhesive networks.Tyrosine phosphorylation of Rac1: a role in regulation of cell spreading Paxillin-kinase-linker tyrosine phosphorylation regulates directional cell migration.Focal adhesion kinase and endothelial cell apoptosis.Deficiency in the LIM-only protein Fhl2 impairs skin wound healing PI3K and Erk MAPK mediate ErbB signaling in Xenopus gastrulation.Disruption of c-Jun reduces cellular migration and invasion through inhibition of c-Src and hyperactivation of ROCK II kinase.Plakoglobin regulates cell motility through Rho- and fibronectin-dependent Src signaling.A biosensor generated via high-throughput screening quantifies cell edge Src dynamics Spatial organization of the extracellular matrix regulates cell-cell junction positioning.Dissecting motility signaling through activation of specific Src-effector complexes Engineering extrinsic disorder to control protein activity in living cells.The GAB2 signaling scaffold promotes anchorage independence and drives a transcriptional response associated with metastatic progression of breast cancer.Migfilin interacts with Src and contributes to cell-matrix adhesion-mediated survival signaling.

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P2860

The interplay between Src and integrins in normal and tumor biology.

http://www.wikidata.org/entity/Q35920891

description

2004 nî lūn-bûn

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2004年の論文

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2004年論文

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2004年論文

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2004年論文

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2004年論文

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2004年論文

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2004年论文

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2004年论文

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2004年论文

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name

The interplay between Src and integrins in normal and tumor biology.

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The interplay between Src and integrins in normal and tumor biology.

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The interplay between Src and integrins in normal and tumor biology.

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The interplay between Src and integrins in normal and tumor biology.

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The interplay between Src and integrins in normal and tumor biology.

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The interplay between Src and integrins in normal and tumor biology.

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The interplay between Src and integrins in normal and tumor biology.

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Martin P Playford

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Michael D Schaller

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P2860

Identification of protein-tyrosine phosphatase 1B as the major tyrosine phosphatase activity capable of dephosphorylating and activating c-Src in several human breast cancer cell lines

Coordinate interactions of Csk, Src, and Syk kinases with [alpha]IIb[beta]3 initiate integrin signaling to the cytoskeleton

Src kinase activation by direct interaction with the integrin beta cytoplasmic domain

Roles of Gab1 and SHP2 in paxillin tyrosine dephosphorylation and Src activation in response to epidermal growth factor

CAS/Crk coupling serves as a "molecular switch" for induction of cell migration.

Identification of p130Cas as a mediator of focal adhesion kinase-promoted cell migration

Recruitment of the Arp2/3 complex to vinculin: coupling membrane protrusion to matrix adhesion

Monoclonal antibodies to individual tyrosine-phosphorylated protein substrates of oncogene-encoded tyrosine kinases.

Increase in activity and level of pp60c-src in progressive stages of human colorectal cancer

Tyrosine phosphorylation of paxillin and pp125FAK accompanies cell adhesion to extracellular matrix: a role in cytoskeletal assembly

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7928-7946

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scholarly article

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10.1038/SJ.ONC.1208080

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48

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