scholarly journals Differential Regulation of Focal Adhesion Kinase and Mitogen-Activated Protein Kinase Tyrosine Phosphorylation During Insulin-Like Growth Factor-I-Mediated Cytoskeletal Reorganization

2002 ◽  
Vol 71 (3) ◽  
pp. 1333-1336 ◽  
Author(s):  
Bhumsoo Kim ◽  
Eva L. Feldman
Keyword(s):  
Growth Factor ◽  
Protein Kinase ◽  
Focal Adhesion Kinase ◽  
Tyrosine Phosphorylation ◽  
Focal Adhesion ◽  
Differential Regulation ◽  
Mitogen Activated Protein Kinase ◽  
Cytoskeletal Reorganization ◽  
Factor I ◽  
Mitogen Activated Protein

Focal adhesion kinase, RhoA, and p38 mitogen‐activated protein kinase modulates apoptosis mediated by angiotensin II AT 2 receptors

2018 ◽  
Vol 120 (2) ◽  
pp. 1835-1849 ◽  
Author(s):  
María J. Manzur ◽  
Milton O. Aguilera ◽  
Mónica L. Kotler ◽  
Walter Berón ◽  
Gladys M. Ciuffo
Keyword(s):  
Angiotensin Ii ◽  
Protein Kinase ◽  
Focal Adhesion Kinase ◽  
Focal Adhesion ◽  
Mitogen Activated Protein Kinase ◽  
Mitogen Activated Protein

scholarly journals Dissociation of mitogen-activated protein kinase activation from p125 focal adhesion kinase tyrosine phosphorylation in Swiss 3T3 cells stimulated by bombesin, lysophosphatidic acid, and platelet-derived growth factor.

1996 ◽  
Vol 7 (12) ◽  
pp. 1865-1875 ◽  
Author(s):  
T Seufferlein ◽  
D J Withers ◽  
D Mann ◽  
E Rozengurt
Keyword(s):  
Protein Kinase ◽  
Tyrosine Phosphorylation ◽  
Focal Adhesion ◽  
Lysophosphatidic Acid ◽  
Mitogen Activated Protein Kinase ◽  
Platelet Derived Growth Factor ◽  
3T3 Cells ◽  
Kinase C ◽  
Mitogen Activated Protein ◽  
Swiss 3T3

The experiments presented here were designed to examine the contribution of p125 focal adhesion kinase (p125FAK) tyrosine phosphorylation to the activation of the mitogen-activated protein kinase cascade induced by bombesin, lysophosphatidic acid (LPA), and platelet-derived growth factor (PDGF) in Swiss 3T3 cells. We found that tyrosine phosphorylation of p125FAK in response to these growth factors is completely abolished in cells treated with cytochalasin D or in cells that were suspended in serum-free medium for 30 min. In marked contrast, the activation of p42mapk by these factors was independent of the integrity of the actin cytoskeleton and of the interaction of the cells with the extracellular matrix. The protein kinase C inhibitor GF 109203X and down-regulation of protein kinase C by prolonged pretreatment of cells with phorbol esters blocked bombesin-stimulated activation of p42mapk, p90rsk, and MAPK kinase-1 but did not prevent bombesin-induced tyrosine phosphorylation of p125FAK. Furthermore, LPA-induced p42mapk activation involved a pertussis toxin-sensitive guanylate nucleotide-binding protein, whereas tyrosine phosphorylation of p125FAK in response to LPA was not prevented by pretreatment with pertussis toxin. Finally, PDGF induced maximum p42mapk activation at concentrations (30 ng/ml) that failed to induce tyrosine phosphorylation of p125FAK. Thus, our results demonstrate that p42mapk activation in response to bombesin, LPA, and PDGF can be dissociated from p125FAK tyrosine phosphorylation in Swiss 3T3 cells.

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