Focal adhesion kinase (p125FAK): A point of convergence in the action of neuropeptides, integrins, and oncogenes

  title={Focal adhesion kinase (p125FAK): A point of convergence in the action of neuropeptides, integrins, and oncogenes},
  author={Ian Zachary and Enrique Rozengurt},
Soft matrix is a natural stimulator for cellular invasiveness
Findings suggest that cell invasion in vivo is a spontaneous cell behavior in response to ECM stiffness, and that ECM softness alone is sufficient to prevent cell-to-cell adherens junction formation and promote MMP activity.
HER-2 Signaling in Human Breast Cancer
Localization of focal adhesion kinase isoforms in cells of the central nervous system
Evidence for LFA‐1/ICAM‐1 dependent stimulation of protein tyrosine phosphorylation in human B lymphoid cell lines during homotypic adhesion
Results suggest that an LFA‐1‐dependent PTK pathway may play an important role in human B cell function, and patients with the leukocyte adhesion defect (LAD) exhibit humoral abnormalities.
Basic fibroblast growth factor promotes adhesive interactions of neuroepithelial cells from chick neural tube with extracellular matrix proteins in culture.
Basic fibroblast growth factor (bFGF) is involved in the developmental regulation of adhesive interactions between neuroepithelial cells and the extracellular matrix, thereby controlling their proliferation, migration and differentiation.
FAK phosphorylation at Ser‐843 inhibits Tyr‐397 phosphorylation, cell spreading and migration
It is shown that FAK phosphorylation at Ser‐843 is strikingly increased when adherent cells are removed from the substratum and held in suspension or by treatment of adherent cells with cytochalasin D, conditions that disrupt the F‐actin cytoskeleton and promote focal adhesion disassembly, suggesting a mechanism of cross‐talk between these phosphorylated sites that could regulate FAK‐mediated cell shape and migration.
Mitogenic signaling pathways induced by G protein‐coupled receptors
Recent advances in defining the pathways that play a role in transducing mitogenic responses induced by GPCR agonists are reviewed.
Controlling Fibronectin Fibrillogenesis Using Visible Light
Pre-exposure of FN to visible light prior to cell seeding thus provides a useful tool to delineate mechanosensitive signaling pathway related to FN fibrillogenesis.
Conditioned medium from rat dental pulp reduces the number of osteoclasts via attenuation of adhesiveness in osteoclast precursors.
CM from dental pulp serves as an inhibitor of osteoclastogenesis by reducing the number and adhesiveness of osteOClast precursors, suggesting novel therapeutic applicability for osteoporosis.


Growth factors and cell proliferation.
Integrin-dependent phosphorylation and activation of the protein tyrosine kinase pp125FAK in platelets
This study provides the first genetic evidence that tyrosine phosphorylation of pp125FAK is dependent on integrin- mediated events, and demonstrates that there is a strong correlation between tyrosines phosphorylated in platelets, and the activation of pp 125FAK-associated phosphorylating activity in vitro.
Regulation of focal adhesion-associated protein tyrosine kinase by both cellular adhesion and oncogenic transformation
It is shown that tyrosineosphorylation of this protein is modulated both by cell adhesion and transformation by pp60v–src, and that these changes in phosphorylation are correlated with increased pp125FAKtyrosine kinase activity.
Tyrosine phosphorylation of paxillin and pp125FAK accompanies cell adhesion to extracellular matrix: a role in cytoskeletal assembly
A role for integrin- mediated tyrosine phosphorylation in the organization of the cytoskeleton as cells adhere to the extracellular matrix is suggested.
Bradykinin and bombesin rapidly stimulate tyrosine phosphorylation of a 120-kDa group of proteins in Swiss 3T3 cells.
It is shown that an increase in tyrosine phosphorylation of a 120-kDa group of proteins is an early protein kinase C-independent cellular signal elicited by both bradykinin and bombesin.
Paxillin is a major phosphotyrosine-containing protein during embryonic development
  • C. Turner
  • Biology
    The Journal of cell biology
  • 1991
The data suggest that the regulated phosphorylation of tyrosine residues on paxillin may perform a critical role in controlling cell and tissue cytoarchitecture rearrangement during vertebrate development.