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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
 
 
 
 

Independent activation of endogenous p21-activated protein kinase-3 ( PAK3) and JNK by thrombin in CCL39 fibroblasts.

Thrombin, a potent mitogen for CCL39 hamster lung fibroblasts, activates the seven membrane-spanning receptor PAR1. To better understand the signaling pathways controlled by this receptor we analyzed a potential downstream effector, p21-activated protein kinase (PAK). Thrombin and PAR1 agonist peptide, as well as serum and lysophosphatidic acid, were found to stimulate HA-mPAK3 activity in CCL39 cells transfected with a plasmid encoding the epitope-tagged kinase. Similar results were obtained using antibodies developed against the endogenous kinase. PAK3 activation is sensitive to pertussis toxin, but insensitive to LY 294002, an inhibitor of phosphatidylinositol 3'-kinase. Thrombin and serum also activate c-jun amino terminal kinase ( JNK). Similar to PAK3 activation, thrombin-stimulated JNK activity is inhibited by pertussis toxin, but not by LY 294002. In a CCL39-derived cell line expressing constitutively active mPAK3 in a tetracyline-dependent manner, induction of PAK activity does not lead to corresponding increases in JNK activity. Our findings indicate that PAK3 is responsive to thrombin and other G protein-coupled receptor systems. Furthermore, our data suggest that in CCL39 cells, JNK activation by thrombin occurs independently of PAK3.[1]

References

  1. Independent activation of endogenous p21-activated protein kinase-3 (PAK3) and JNK by thrombin in CCL39 fibroblasts. Malcolm, K.C., Chambard, J.C., Grall, D., Pouysségur, J., van Obberghen-Schilling, E. J. Cell. Physiol. (2000) [Pubmed]
 
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