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Example sentences for: fak
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Furthermore, we found that the tyrosine phosphorylated Cas SD competed effectively with the endogenous Cas for binding to v-crk and endogenous c-crk, while not affecting tyrosine phosphorylation of proposed upstream proteins such as Fak and endogenous Cas.
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 of the established in vivo substrates of PTEN, FAK, is known to play a major role in growth-regulatory signal transduction initiated by cell surface integrin receptors [ 48 49 ] . As we observe a correlation between increased PTEN activity and decreased levels of FAK phosphorylation (compare Figure 4Band Figure 5), it is likely that the dephosphorylation of FAK in response to the disruption of cell-matrix interactions is accomplished by increased PTEN activity.
In addition, we determined if tyrosine phosphorylation of endogenous FAK and endogenous Cas was affected by the presence of the chimera.
The underlying processes involve the stimulation of expression of p27 Kip1and the dephosphorylation of FAK.
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