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Human FAK Protein expressed in HEK-293 Cells - ABIN2720714
Banerjee, de Freitas, Friggeri, Zmijewski, Liu, Abraham: Intracellular HMGB1 negatively regulates efferocytosis. in Journal of immunology (Baltimore, Md. : 1950) 2011
MPAP suppressed cancer cell proliferation and the phosphorylation of FAK1. Combined treatment with MPAP and irradiation (IR) showed enhanced suppression of cancer cell proliferation in wild-type p53 (show TP53 Proteins) cells and more intense suppression in p53 (show TP53 Proteins)-null cells
Optogenetic control of FAK signaling has been described.
results suggest that W2 suppresses cancer cell migration and invasion by inhibiting FAK/STAT3 (show STAT3 Proteins) signaling and STAT3 (show STAT3 Proteins) translocation to the nucleus in monomorphic malignant human glioma cells.
these results suggest that Ascochlorin inhibits cell migration and invasion by blocking FAK and JAK (show JAK3 Proteins)/STAT (show STAT1 Proteins) signaling, resulting in reduced MMP-2 (show MMP2 Proteins) activity.
High levels of phosphorylated tyrosine-397 FAK in the nucleus of patient-derived melanoma tissues.
The RNA-editing enzyme ADAR (show ADAR Proteins) promotes lung adenocarcinoma migration and invasion by stabilizing FAK.
The ectopic overexpression of miR-379 inhibited cell migration, invasion and EMT progress, while downregulated miR-379 reversed the effect. In addition, miR-379 regulated the focal adhesion kinase (FAK) by directly binding to its 3'-UTR, resulting in suppression of AKT signaling. In clinical samples of gastric cancer (GC), miR-379 inversely correlated with FAK, which was upregulated in GC.
Building upon previous work suggesting that FAK-Akt1 (show AKT1 Proteins) binding is mediated by the FAK F1 lobe, we demonstrated that independently expressing the F1 domain in human Caco-2 or murine CT-26 (show DDX53 Proteins) colon cancer cells by transient or stable inducible plasmid expression respectively prevents the stimulation of cancer cell adhesion by increased extracellular pressure.
functional activation of FAK1 in metastases and provide preclinical rationale for targeting this kinase in the setting of advanced ccRCC
this study shows that simultaneous deactivation of FAK and Src (show SRC Proteins) improves the pathology of hypertrophic scar
evidence that despite the fact that FAK is in the active, open conformation at CAs (show CSE1L Proteins), its kinase activity is dispensable for ciliogenesis and ciliary function revealing that FAK plays a scaffolding role in multiciliated cells.
FAK is required for external force-induced spindle reorientation, suggesting that FAK's involvement in this process stems from a role in the transduction of external forces to the cell cortex.
FAK is required for tension-dependent organization of collective cell movements in Xenopus mesendoderm.
work identifies new roles for the FERM domain in the regulation of the dynamics of FAK on its signaling complexes in vivo and in vitro and identifies epiboly as the earliest developmental process in which FAK plays a crucial role during development
These data suggest an important role for the FERM domain in the activation of FAK.
FAK phosphorylation at Y861 is essential for lamellipodial protrusion induced by BDNF (show BDNF Proteins), while phosphorylation at Y925 controls the rate of point contact turnover.
Data imply that FAK plays an essential role in chamber outgrowth and looping morphogenesis.
FAK is required for proper topographic positioning of retinal axons along the anterior-posterior axis of the optic tectum in Xenopus and zebrafish, a guidance decision mediated in part by A-type ephrins.
RhoA (show RHOA Proteins) and membrane fluidity mediates the spatially polarized Src (show SRC Proteins)/FAK activation in response to shear stress.
XIAP (show XIAP Proteins) plays an essential role in shear stress-stimulated FAK phosphorylation.
mitochondrial oxidants generated in response to endothelial strain trigger FAK phosphorylation through a signaling pathway that involves protein kinase C
These results suggest that TGF-beta1 (show TGFB1 Proteins)-induced monolayer permeability involves focal adhesion and cytoskeletal rearrangement through both FAK/Src (show SRC Proteins)-dependent and -independent pathways.
Results suggest focal adhesion kinase is involved in thrombospondin-1 (show THBS1 Proteins)-induced vascular smooth muscle cell migration.
In conclusion, our observations reveal that PRRSV triggers the activation of FAK-PI3K-AKT-Rac1 signaling pathway to facilitate its entry into cells.
Data suggest that focal adhesion kinase (FAK)-SMAD 2/3 mediate signal crosstalk between type II collagen and TGF-beta1 and regulate glycosaminoglycan secretion in chondrocytic cells.
FAK is essentially required in chondrocyte communication with type II collagen (show COL2A1 Proteins) by regulating type II collagen (show COL2A1 Proteins) expression and cell proliferation.
these data provide mechanistic insight into how FAK controls the tumor immune environment, namely, through a transcriptional regulatory network mediated by nuclear IL-33 (show IL33 Proteins).
These findings suggest that NG2 (show Vcan Proteins) expression mediates inflammatory reactions and neurodegeneration in microglial cells in response to central nervous system injury, potentially by regulating FAK phosphorylation.
FAK tyrosine 397 autophosphorylation is required for FAK function and is positively regulated by MYO1E (show MYO1E Proteins).
IP6K1 (show IP6K1 Proteins) physiologically regulates neuronal migration by binding to alpha-actinin (show ACTN1 Proteins) and influencing phosphorylation of both FAK and alpha-actinin (show ACTN1 Proteins) through its product 5-diphosphoinositol pentakisphosphate.
The results suggest that FAK is not required for monocyte migration to the perivascular space and that vascular remodeling following arterial occlusion occurs independently of myeloid specific FAK.
These results provide a molecular explanation of how initiation of B cell activation (show BLNK Proteins) discriminates substrate stiffness through a PKCbeta-mediated FAK activation dependent manner.
An FAK-YAP (show YAP1 Proteins)-mTOR (show FRAP1 Proteins) Signaling Axis Regulates Stem Cell-Based Tissue Renewal in Mice.
loss of FAK signaling during endoplasmic reticulum stress causes mitochondrial dysfunction by reducing the protective effects of mitochondrial STAT3 (show STAT3 Proteins), leading to endothelial cell death.
Hypoxia activated the focal adhesion kinase (FAK) pathway through upregulation of BNIP3, while FAK inhibition attenuated hypoxic keratinocyte migration.
These data support a crucial role for miR (show MYLIP Proteins)-27 in promoting chondrogenic differentiation in the pharyngeal arches through regulation of FAK.
findings highlight an essential role of Paxillin (show PXN Proteins) and FAK in controlling cardiac contractility via the recruitment of Vinculin (show VCL Proteins) to mechano-sensitive sites in cardiomyocytes.
Data indicate that focal adhesion kinase (FAK) activity may be a mediator of the integrin alpha5/Fn1 interaction during zebrafish lens fiber morphogenesis.
Focal adhesion kinase (FAK) mediates regulation of growth cone adhesion in the optic tectum of zebrafish.
presynaptic FAK signaling may be disrupted, causing abnormal synaptic growth and transmission in the NF1 (show NF1 Proteins) genetic
Fak56 may play a subtle role in the negative regulation of integrin adhesion
Fak56D mutation causes severe disruption of the optic stalk structure. These phenotypes were completely rescued by Fak56D transgene expression in the SG cells but not in photoreceptor cells.
An intron loss of Dfak gene in species of the Drosophila melanogaster subgroup.
Together these findings suggest that modulation of Fak56 function is important for action potential propagation and Ca2 (show CA2 Proteins)+-regulated neuromuscular transmission in vivo.
Data show that Fak56 is required to restrict larval neuromuscular junctions (NMJ)growth during NMJ development and mediates an extracellular signal through the integrin receptor.
This gene encodes a cytoplasmic protein tyrosine kinase which is found concentrated in the focal adhesions that form between cells growing in the presence of extracellular matrix constituents. The encoded protein is a member of the FAK subfamily of protein tyrosine kinases but lacks significant sequence similarity to kinases from other subfamilies. Activation of this gene may be an important early step in cell growth and intracellular signal transduction pathways triggered in response to certain neural peptides or to cell interactions with the extracellular matrix. Several transcript variants encoding different isoforms have been found for this gene, but the full-length natures of only three of them have been determined.
, FAK-related non-kinase polypeptide
, PTK2 protein tyrosine kinase 2
, focal adhesion kinase 1
, focal adhesion kinase-related nonkinase
, protein phosphatase 1 regulatory subunit 71
, protein phosphatase 1, regulatory subunit 71
, focal adhesion kinase pp125FAK
, protein-tyrosine kinase 2
, focal adhesion kinase
, focal ashension kinase 1
, protein tyrosine kinase 2.1
, focal adhesion kinase homolog