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Focal adhesion kinase (FAK) is a cytoplasmic tyrosine kinase implicated in the signal transduction pathways initiated by integrins. However, we havc previously found that platelet-derived growth factor (PDGF) could stiinulate thc association of FAK with phosphatidylinositol 3-kinase in NIH 3T3 cclls [Chcn, H.-C. & Guan, J.-L. (1994) J, Bid. Chwz. 269, 31 229-31 2331, suggesting that FAK might participate in some of the cellular effects of the growth factors in modulating cell morphology and migration. In this report, wc describc the association of FAK with a 200-kDa protein (pp200) that is tyrosine phosphorylated in response to PDCF stirnulation i n N l l i 3T3 cells. Although the idenlily of pp200 is unknown at prescnt, we have excluded the possibilities that it is the PDGF receptor /j, tcnsin, talin, myosin or the guanosine-triophosphatase-activatiiig-protein-iissociatcd pi 40 protcin. Fux1licrmore, we found that thc tyrosine phosphorylation of FAK-associated pp200 upon PDGF stimulation is largely independent of ccll adhesion or the integrity of the cytoskeleton. Therefore, pp200 and its interactions with FAK may also be involved in growth-factor-inciuced ccllular effccts such as the moclulation of ccll adhesion or cell migration via cytoskelctal reorganization or disruption of focnl adhesions.Keywords: focal adhesion kiniise; platelet-derived growth factor; pp200; tyrosine phosphorylation ; signal transduction.In multiccllular organisms, the growth, migration, and differentiiltion of individual cells is tightly controlled by their extracellular environments. Two major classes of controlling cornponents are diffusible growth factors and insoluble extracellular matrix (ECM) proteins, which often influence cellular behavior cooperativcly [I -41. Despite our undersvanding of signal transduction pathways initiated by growth faciors and ECM proteins, little is known about potential interactions of these two pathways. For example, platelet-derived growth factor (PDGF) has been reported to induce changcs in cell morphology and stiniulate chemotaxis [5-91 in addition to its rnitogenic activity. Rapid progress has been made in recent years in elucidating the molecular cascade involved in the mitogenic activity of PDGF [S, 10-121, which includes activation and autophorylation of the PDGF receptor upon ligand stimuliition and recruitment of intracellular signaling molecules containing src-homology-:! (SH2) domains to the plasrna incmbranc. However, the molecular cascades leading to thc PDGf;-mediated modulation of cell adhesion and cytoskeletal organization are less understood.Focal adhesion kinase (FAK) is a cytoplasmic tyrosine kinase localizcd in focal contacts 113, 141, which has been implicatcd to play a role in regulating cellular morphology and migration in response to cell adhesion to ECM protcins. Cell attacliment to fibronectin-coated surfaces or integrin clustering by antibodies rapidly induces FAK tyrosine phosphorylation I IS-21 I.In both fibroblasts and platelets, the tyrosine kinasc activity of FAK is als...
Focal adhesion kinase (FAK) is a cytoplasmic tyrosine kinase implicated in the signal transduction pathways initiated by integrins. However, we havc previously found that platelet-derived growth factor (PDGF) could stiinulate thc association of FAK with phosphatidylinositol 3-kinase in NIH 3T3 cclls [Chcn, H.-C. & Guan, J.-L. (1994) J, Bid. Chwz. 269, 31 229-31 2331, suggesting that FAK might participate in some of the cellular effects of the growth factors in modulating cell morphology and migration. In this report, wc describc the association of FAK with a 200-kDa protein (pp200) that is tyrosine phosphorylated in response to PDCF stirnulation i n N l l i 3T3 cells. Although the idenlily of pp200 is unknown at prescnt, we have excluded the possibilities that it is the PDGF receptor /j, tcnsin, talin, myosin or the guanosine-triophosphatase-activatiiig-protein-iissociatcd pi 40 protcin. Fux1licrmore, we found that thc tyrosine phosphorylation of FAK-associated pp200 upon PDGF stimulation is largely independent of ccll adhesion or the integrity of the cytoskeleton. Therefore, pp200 and its interactions with FAK may also be involved in growth-factor-inciuced ccllular effccts such as the moclulation of ccll adhesion or cell migration via cytoskelctal reorganization or disruption of focnl adhesions.Keywords: focal adhesion kiniise; platelet-derived growth factor; pp200; tyrosine phosphorylation ; signal transduction.In multiccllular organisms, the growth, migration, and differentiiltion of individual cells is tightly controlled by their extracellular environments. Two major classes of controlling cornponents are diffusible growth factors and insoluble extracellular matrix (ECM) proteins, which often influence cellular behavior cooperativcly [I -41. Despite our undersvanding of signal transduction pathways initiated by growth faciors and ECM proteins, little is known about potential interactions of these two pathways. For example, platelet-derived growth factor (PDGF) has been reported to induce changcs in cell morphology and stiniulate chemotaxis [5-91 in addition to its rnitogenic activity. Rapid progress has been made in recent years in elucidating the molecular cascade involved in the mitogenic activity of PDGF [S, 10-121, which includes activation and autophorylation of the PDGF receptor upon ligand stimuliition and recruitment of intracellular signaling molecules containing src-homology-:! (SH2) domains to the plasrna incmbranc. However, the molecular cascades leading to thc PDGf;-mediated modulation of cell adhesion and cytoskeletal organization are less understood.Focal adhesion kinase (FAK) is a cytoplasmic tyrosine kinase localizcd in focal contacts 113, 141, which has been implicatcd to play a role in regulating cellular morphology and migration in response to cell adhesion to ECM protcins. Cell attacliment to fibronectin-coated surfaces or integrin clustering by antibodies rapidly induces FAK tyrosine phosphorylation I IS-21 I.In both fibroblasts and platelets, the tyrosine kinasc activity of FAK is als...
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