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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
The interaction between FAK and tetraspan proteins in physiological and pathological conditions is reviewed.
BKCa (show KCNMA1 Proteins) has a role in promoting growth and metastasis of prostate cancer through facilitating the coupling between alphavbeta3 integrin and FAK
Proteomic analysis identified PTK2/FAK overexpression is a biomarker of radioresistance in locally advanced HNSCC, and PTK2/FAK inhibition radiosensitized HNSCC cells.
FAK-Src (show SRC Proteins)-Paxillin (show PXN Proteins) system is a marker of unfavorable prognosis for human Neuroblastoma (show ARHGEF16 Proteins) patients but also a promising therapeutic target.
IGF-II siRNA inactivates the FAK/PI3K (show PIK3CA Proteins)/Akt (show AKT1 Proteins) signaling pathway, and further reduces cell proliferation, N-ras (show NRAS Proteins) and C-myc (show MYC Proteins) levels in SMMC-7721 cells.
The purpose of this study was to determine the maximum tolerated dose (MTD (show MT1E Proteins)), safety, pharmacokinetics (PK), and pharmacodynamics (PD) of the FAK inhibitor, GSK2256098, in cancer patients.GSK2256098 has an acceptable safety profile, has evidence of target engagement at doses at or below the MTD (show MT1E Proteins), and has clinical activity in patients with mesothelioma, particularly those with merlin (show NF2 Proteins) loss
Studies suggest that signaling pathways downstream of activated FAK including paxillin (show PXN Proteins) will be important to study in the context of FAK inhibition and other therapeutics to identify novel biomarkers.
The levels of phosphorylated FAK (Tyr397 and Tyr925) were increased after overexpressing Lasp2 (show NEBL Proteins) and were downregulated by transfecting Lasp2 (show NEBL Proteins)-siRNA.
Human pluripotent stem cells promote the expression of integrin alpha6beta1, and nuclear localization and inactivation of FAK to supports stem cell self-renewal.
In contrast to mice, the analysis of human olfactory bulbs revealed a late activation of FAK in advanced AAlzheimer's disease stages, whereas ERK1/2 activation was enhanced across AD staging
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.
Irradiation coupled with JNK inhibition in beta1 integrin -/- transgenic adenocarcinoma of prostate (TRAMP) leads to increased levels of nuclear focal adhesion kinase (FAK) in tumor cells.
Ablation of Cyclophilin D (show PPIF Proteins) Results in an Activation of FAK, Akt (show AKT1 Proteins), and ERK (show EPHB2 Proteins) Pathways in the Mouse Heart.
FAK loss in calvarial preosteoblasts had no adverse effect on their proliferation and osteogenic differentiation and these cells had intact Wnt (show WNT2 Proteins)/beta-catenin (show CTNNB1 Proteins) signaling.
Ambra1 (show AMBRA1 Proteins) binds to both FAK and Src (show SRC Proteins) in cancer cells. When FAK is present, Ambra1 (show AMBRA1 Proteins) is recruited to focal adhesions, promoting FAK-regulated cancer cell direction-sensing and invasion. However, when Ambra1 (show AMBRA1 Proteins) cannot bind to FAK, abnormally high levels of phospho-Src (show SRC Proteins) and phospho-FAK accumulate at focal adhesions, positively regulating adhesion and invasive migration.
In mouse olfactory bulbs, beta-amyloid induced an inactivation of focal adhesion kinase (FAK) together with a transient activation of MEK1/2, leading to inactivation of ERK1/2.
Osteoprotegerin (show TNFRSF11B Proteins) facilitates pulmonary arterial hypertension pathogenesis by regulating pulmonary arterial smooth muscle cell proliferation via integrin alphavbeta3 (show ITGAV Proteins)/FAK/AKT (show AKT1 Proteins) signaling pathway.
High FAK expression is associated with skin squamous cell carcinoma.
In cardiomyocytes exposed to biomechanical stimulation, FAK accumulates in the nucleus, binds to and upregulates the transcriptional activity of MEF2c (show MEF2C Proteins) through an interaction with the FAK focal adhesion targeting (FAT) domain.
FAK-knockout mice were shorter and showed reduced bone volume. Disruptions of FAK function in osteoblasts reduced mRNA and protein expression of Runx2 (show RUNX2 Proteins) Osterix (show SP7 Proteins) and collagen-1.
The remodeling of the stromal matrix by CAFs has been shown to increase tumor rigidity to indirectly regulate FAK Y397 phosphorylation in tumor cells to promote their growth and invasion. Accordingly, the Hic-5(-/-);PyMT tumor cells exhibited a reduction in FAK Y397 phosphorylation. Isolated Hic-5(-/-);PyMT CAFs were defective in stress fiber organization and exhibited reduced contractility
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
, activated Cdc42 kinase-like
, tyrosine kinase
, focal adhesion kinase homolog