منابع مشابه
Regulation of Raf-Akt Cross-talk.
We have recently shown that the Ras-Raf-MEK-ERK and phosphatidylinositol 3-kinase (PI3K)-Akt signaling pathways can cross-talk in the human breast cancer cell line MCF-7. High Raf activity induces growth arrest and differentiation in these cells, whereas high PI3K/Akt activity correlates with cell survival and proliferation. Here we show that the Raf-Akt cross-talk is regulated in a concentrati...
متن کاملA Mathematical Modeling of Signal Transduction Cascade on Raf-Akt Cross-Talk
MAPK signaling cascade initiated by the activation of EGF receptor (EGFR) has been experimentally well studied and analyzed by mathematical modeling extensively [1, 3, 5]. Recently, several studies showed that some of growth hormone-stimulated membrane tyrosine kinase receptors interact with Shc adaptor protein and phosphatidylinositol 3’-kinase (PI3K), and consequently PI3K-activated Akt inhib...
متن کاملRegulation of Raf-1 kinase by TNF via its second messenger ceramide and cross-talk with mitogenic signalling.
Raf-1 kinase is a central regulator of mitogenic signal pathways, whereas its general role in signal transduction of tumour necrosis factor (TNF) is less well defined. We have investigated mechanisms of Raf-1 regulation by TNF and its messenger ceramide in cell-free assays, insect and mammalian cell lines. In vitro, ceramide specifically bound to the purified catalytic domain and enhanced assoc...
متن کاملAKT3 promotes prostate cancer proliferation cells through regulation of Akt, B-Raf & TSC1/TSC2
The qRT-PCR analysis of 139 clinical samples and analysis of 150 on-line database clinical samples indicated that AKT3 mRNA expression level was elevated in primary prostate tumors. Immunohistochemical staining of 65 clinical samples revealed that AKT3 protein expression was higher in prostate tumors of stage I, II, III as compared to nearby normal tissues. Plasmid overexpression of AKT3 promot...
متن کاملNegative regulation of the serine/threonine kinase B-Raf by Akt.
B-Raf contains multiple Akt consensus sites located within its amino-terminal regulatory domain. One site, Ser(364), is conserved with c-Raf but two additional sites, Ser(428) and Thr(439), are unique to B-Raf. We have investigated the role of both the conserved and unique phosphorylation sites in the regulation of B-Raf activity in vitro and in vivo. We show that phosphorylation of B-Raf by Ak...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 2002
ISSN: 0021-9258
DOI: 10.1074/jbc.m111974200