Negative regulation of the serine/threonine kinase B-Raf by Akt.
作者： Kun-Liang Guan , Claudia Figueroa , Teresa R Brtva , Tianquan Zhu , Jennifer Taylor
关键词: Protein-Serine-Threonine Kinases 、 Serine 、 Protein kinase B 、 Kinase 、 PI3K/AKT/mTOR pathway 、 Molecular biology 、 Serine/threonine-specific protein kinase 、 Phosphorylation 、 Chemistry 、 Cell biology 、 AKT1
摘要: 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 phosphorylation in regulation activity vitro vivo. show that by occurs at residues domain, sites. The alteration serine alanines results a progressive increase enzymatic Furthermore, expression inhibits epidermal growth factor-induced inhibition LY294002 up-regulates activity, suggesting negatively regulates Our demonstrate can be regulated through domain This cross-talk between serine/threonine kinases likely play an important modulating signaling specificity Ras/Raf pathway promoting biological outcome.
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