Regulation of the PH-domain-containing tyrosine kinase Etk by focal adhesion kinase through the FERM domain

@article{Chen2001RegulationOT,
  title={Regulation of the PH-domain-containing tyrosine kinase Etk by focal adhesion kinase through the FERM domain},
  author={Riyan Chen and Oekyung Kim and Ming Li and Xinsheng Xiong and Jun-Lin Guan and Hsing-Jien Kung and Hegang Chen and Yoji Shimizu and Yun Qiu},
  journal={Nature Cell Biology},
  year={2001},
  volume={3},
  pages={439-444}
}
Etk/BMX, a member of the Btk family of tyrosine kinases, is highly expressed in cells with great migratory potential, including endothelial cells and metastatic carcinoma cell lines. Here, we present evidence that Etk is involved in integrin signalling and promotes cell migration. The activation of Etk by extracellular matrix proteins is regulated by FAK through an interaction between the PH domain of Etk and the FERM domain of FAK. The lack of Etk activation by extracellular matrix in FAK-null… 
Regulation of Focal Adhesion Kinase by Its Amino-Terminal Domain through an Autoinhibitory Interaction
TLDR
A working model for activation of FAK in cell adhesion is proposed, suggesting that FAK could be regulated by molecular interactions with the amino terminus, which can act in trans to inhibit FAK phosphorylation when expressed in mammalian cells or to directly inhibitFAK activity in vitro.
Direct Interaction of the N-terminal Domain of Focal Adhesion Kinase with the N-terminal Transactivation Domain of p53*
TLDR
The results of the FAK and p53 interaction study strongly support the conclusion that FAK can suppress p53-mediated apoptosis and inhibit transcriptional activity of p53.
Phosphorylation of focal adhesion kinase on tyrosine 194 by Met leads to its activation through relief of autoinhibition
TLDR
This study provides the first example to explain how FAK is activated by receptor tyrosine kinases by demonstrating that growth factor receptors directly phosphorylate FAK on Tyr194 in the FERM domain.
p130Cas Couples the Tyrosine Kinase Bmx/Etk with Regulation of the Actin Cytoskeleton and Cell Migration*
TLDR
These studies suggest that Bmx-Cas interaction, phosphorylation of Cas by Bmx, and subsequent Cas·Crk complex formation functionally couple Bmx to the regulation of actin cytoskeleton and cell motility.
Crystal Structure of the FERM Domain of Focal Adhesion Kinase*
TLDR
Two crystal structures of an NH2-terminal fragment of avian FAK containing the FERM domain and a portion of the regulatory linker that connects the F ERM and kinase domains are reported, suggesting the possibility that protein interactions of the FAK FERm domain can be regulated by binding of Src kinases to the linker segment.
Bi-directional Regulation between Tyrosine Kinase Etk/BMX and Tumor Suppressor p53 in Response to DNA Damage*
TLDR
It is proposed that the stoichiometry between p53 and the Tec family kinases in a given cell type may determine its sensitivity to chemotherapeutic drugs.
Direct Interaction of Focal Adhesion Kinase (FAK) with Met Is Required for FAK To Promote Hepatocyte Growth Factor-Induced Cell Invasion
TLDR
It is reported that FAK directly interacts with the hepatocyte growth factor receptor c-Met, providing evidence that constitutive Met-FAK interaction may be a critical determinant for tumor cells to acquire invasive potential.
Residues within the First Subdomain of the FERM-like Domain in Focal Adhesion Kinase Are Important in Its Regulation*
TLDR
A role is suggested for the first FAK subdomain of the FERM domain in its normal regulation and function in the cell, and the K38A mutation weakens the interaction between the amino terminus of FAK and its own kinase domain, and disrupts the ability of the aminoterminus to inhibit the phosphorylation ofFAK in trans.
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It is reported here that overexpression of FAK in CHO cells increased their migration on fibronectin, and a mutation of the major autophosphorylation site Y397 in FAK abolished its ability to stimulate cell migration, while phosphorylation in a kinase-defective FAK by endogenous FAK led to increased migration.
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TLDR
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TLDR
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TLDR
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TLDR
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EtkyBmx, a tyrosine kinase with a pleckstrin-homology domain, is an effector of phosphatidylinositol 3*-kinase and is involved in interleukin 6-induced neuroendocrine differentiation of prostate cancer cells (cytokineysignal transductionyphosphatidylinositidesyLNCaP)
TLDR
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