Focal adhesion kinase has four defined regions, or tertiary structure domains.

Extracellular matrix survival signals transduced by focal adhesion kinase suppress p53-mediated apoptosis.

TGF-β has been shown to influence the plasticity of cells through integrin and focal adhesion kinase.

The specific protein affected by MIT is called focal adhesion kinase, or FAK.

In particular, Dr. Schlaepfer is well known for his studies on focal adhesion kinase (FAK).

The protein plays a role in the integrin signaling pathway and cell migration by binding with focal adhesion kinase (FAK).

Integrin-mediated signal transduction linked to Ras Pathway by Grb2 Binding to Focal adhesion kinase.

Among the scientific community, pp125 is also referred to as FAK (focal adhesion kinase), due to its aforementioned presence in cellular focal adhesions.

It mediates apoptosis by cleavage of focal adhesion kinase through up-regulation of Fas ligand expression in human melanoma cells.

Secreted LOX is responsible for the invasive properties of hypoxic cancer cells through focal adhesion kinase activity and cell-to-matrix adhesion.

ROS can also promote migration by augmenting phosphorylation of the focal adhesion kinase (FAK) p130Cas and paxilin.

Rho family GTPases and focal adhesion kinase (FAK) activate cyclin D gene in response to integrin.

Macrophage inhibitory cytokine-1 (MIC-1) stimulates the focal adhesion kinase (FAK) signaling pathway which leads to prostate cancer cell growth and survival.

Many other intracellular signalling proteins, such as focal adhesion kinase, bind to and associate with this integrin-adapter protein-cytoskeleton complex, and this forms the basis of a focal adhesion.

Antibodies against cell cycle-regulatory proteins as well as those against focal adhesion kinase were purchased from Santa Cruz Biotechnology, Inc. (Santa Cruz, CA).

YopH acts on host focal adhesion sites by dephosphorylating several phosphotyrosine residues on focal adhesion kinase (FAK) and the focal adhesion proteins paxillin and p130.

Angiostatin fragments contain kringle domains which exert their inhibitory activity at several different levels; they inhibit endothelial cell migration and proliferation, increase apoptosis, and modulate the activity of focal adhesion kinase (FAK).

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 ] .

Cell signaling and function As a cell adhesive substrate, CYR61 induces the activation of focal adhesion kinase, paxillin, RAC, and sustained activation of MAPK/ERK1-2.

First, PTEN's protein phosphatase activity is able to down-regulate focal adhesion kinase (FAK) phosphorylation, which leads to the inactivation of the Ras/MAP kinase pathway [ 19 20 21 ] .

These act by regulating kinases such as FAK (focal adhesion kinase) and Src kinase family members to phosphorylate substrates such as p130CAS thereby recruiting signaling adaptors such as CRK.

HA's interaction with CD44 activates focal adhesion kinase (FAK), an important molecule in the process of cell motility by coordinating dissolution of the focal adhesions at the leading edge of the cell and formation at the lagging edge.

Integrin-mediated tumor cell adhesion to ECM proteins can trigger signal transduction and cause upregulation of gene expression, increased tyrosine phosphorylytion of the focal adhesion kinase, and activation and nuclear translocation of mitogen-activated protein (MAP) kinases.

The attractive cues mediated by Semaphorins are not well understood at the moment; however, protein kinase focal adhesion kinase (FAK) and MAP Kinase (MAPK) have been implicated in mediating downstream attractive signaling upon Semaphorin receptor stimulation.