Words similar to fak
Example sentences for: fak
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Indeed, TGFβ 1 antibodies, cytochalasin D and BAPTA-AM [ 66 ] abolished the association on the cytoskeleton connected with integrin α V β 6 and activation of p125 FAK.
TGFβ 1 bound to α V β 6 -integrin in these cells as well, and this interaction resulted both in an immobilization of p130Cas and SOS1/2 and in tyrosine phosphorylation of cytoskeleton-associated proteins such as p125FAK.
Beatrice Knudsen, Weill Medical College of Cornell University, NY, NY); anti-FAK and anti-Cas (Transduction Laboratories, Lexington, KY).
The cell surface expressed integrins can control this process by physically interacting with the extracellular matrix proteins and other cell surface proteins on endothelial cells lining the blood vessel wall [ 1 ] . These integrins signal adhesion and migration by communicating with several tyrosine kinases inside the cell, including the Focal Adhesion Kinase (FAK) and Src family kinases [ 1 2 ] . Src kinases control the activation of FAK, as well as the tyrosine phosphorylation of critical substrates that regulate adhesion and migration [ 3 ] . Indeed, colon cancer cells with high metastatic potential have elevated levels of Src activity or activating mutations in the Src gene [ 4 5 ] . One Src substrate that is involved in regulating an important signaling node in this process is the adaptor protein p130 cas (Cas) [ 6 7 8 9 10 ] . Cas appears to play a central role in the transformation process by several oncogenes including ras, ornithine decarboxylase (ODC), v-Src, v-crk, and Bcr-Abl, as these tumors all have elevated levels of tyrosine phosphorylated Cas [ 6 11 12 13 ] . Cells from mice that lack Cas have much reduced migration and are resistant to transformation by v-Src, while expression of Cas anti-sense RNA in cells transformed with ras, v-Src or ODC result in reversion of the transformed phenotype [ 11 14 15 ] . Furthermore, increased expression of Cas can rescue cell migration and adhesion in cells expressing the tumor suppressor PTEN, and can enhance cell migration and adhesion in normal cells, with a major role being played by the substrate domain [ 16 17 ] .
One is a marked phosphorylation of p125 FAK.
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