The activation of protein kinase B by H2O2 or heat shock is mediated by phosphoinositide 3-kinase and not by mitogen-activated protein kinase-activated protein kinase-2
نویسندگان
چکیده
منابع مشابه
TAK1 mitogen-activated protein kinase kinase kinase is activated by autophosphorylation within its activation loop.
TAK1, a member of the mitogen-activated kinase kinase kinase family, is activated in vivo by various cytokines, including interleukin-1 (IL-1), or when ectopically expressed together with the TAK1-binding protein TAB1. However, this molecular mechanism of activation is not yet understood. We show here that endogenous TAK1 is constitutively associated with TAB1 and phosphorylated following IL-1 ...
متن کاملActivation of mitogen-activated protein kinase (mitogen-activated protein kinase/extracellular signal-regulated kinase) cascade by aldosterone.
Aldosterone in some tissues increases expression of the mRNA encoding the small monomeric G protein Ki-RasA. Renal A6 epithelial cells were used to determine whether induction of Ki-ras leads to concomitant increases in the total as well as active levels of Ki-RasA and whether this then leads to subsequent activation of its effector mitogen-activated protein kinase (MAPK/extracellular signal-re...
متن کاملberberine induced apoptosis of human osteosarcoma cells by inhibiting phosphoinositide 3 kinase/protein kinase b (pi3k/akt) signal pathway activation
background: osteosarcoma is a malignant tumor with high mortality but effective therapy has not yet been developed. berberine, an isoquinoline alkaloid component in several chinese herbs including huanglian, has been shown to induce growth inhibition and the apoptosis of certain cancer cells. the aim of this study was to determine the role of berberine on human osteosarcoma cell lines u2os and ...
متن کاملRedox-dependent dimerization of p38α mitogen-activated protein kinase with mitogen-activated protein kinase kinase 3
The kinase p38α MAPK (p38α) plays a pivotal role in many biological processes. p38α is activated by canonical upstream kinases that phosphorylate the activation region. The purpose of our study was to determine whether such activation may depend on redox-sensing cysteines within p38α. p38α was activated and formed a disulfide-bound heterodimer with MAP2K3 (MKK3) in rat cardiomyocytes and isolat...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Biochemical Journal
سال: 1998
ISSN: 0264-6021,1470-8728
DOI: 10.1042/bj3360241