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Author: Nosaka Y. Arai A. Kanda E. Akasaki T. Sumimoto H. Miyasaka N. Miura O.
Publisher: Elsevier
ISSN: 0006-291X
Source: Biochemical and Biophysical Research Communications, Vol.285, Iss.3, 2001-07, pp. : 675-679
Disclaimer: Any content in publications that violate the sovereignty, the constitution or regulations of the PRC is not accepted or approved by CNPIEC.
Abstract
Tumor necrosis factor α (TNFα) activates various signal transduction pathways including those involving phosphatidylinositol 3-kinase (PI3K), extracellular signal-regulated kinases (Erk), c-Jun N-terminal protein kinases (JNK), and p38 kinases. Using the Rac binding domain of PAK (PAK-RBD) as an activation-specific probe, here we demonstrate that TNFα very rapidly and transiently activates the Rho family GTPase Rac in L929 cells. The PI3K inhibitor LY294002 significantly inhibited TNFα activation of Rac as well as Erk and abolished that of the PI3K target Akt, without showing any inhibitory effects on JNK and p38 activation. Furthermore, TNFα activation of Erk was abolished by a dominant negative Rac mutant, Rac17N, or by an activated Rac mutant, Rac12V. These findings suggest that Rac is activated by a mechanism that is at least partly dependent on PI3K in TNFα stimulated cells and plays a critical role in activation of the Erk signaling pathway.
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