Are zinc-finger domains of protein kinase C dynamic structures that unfold by lipid or redox activation?
Are zinc-finger domains of protein kinase C dynamic structures that unfold by lipid or redox activation?
复制标题
蛋白激酶 C 的锌指结构域是通过脂质或氧化还原激活而展开的动态结构吗？
DOI：
10.1089/ars.2010.3773
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发表时间：
2011
影响因子：
6.6
通讯作者：
Hammerling,Ulrich
中科院分区：
文献类型：
--
作者：
Zhao,Feng;Ilbert,Marianne;Varadan,Ranjani;Cremers,ClaudiaM;Hoyos,Beatrice;Acin-Perez,Rebeca;Vinogradov,Valerie;Cowburn,David;Jakob,Ursula;Hammerling,Ulrich
Protein kinase C (PKC) is activated by lipid second messengers or redox action, raising the question whether these activation modes involve the same or alternate mechanisms. Here we show that both lipid activators and oxidation target the zinc-finger domains of PKC, suggesting a unifying activation mechanism. We found that lipid agonist-binding or redox action leads to zinc release and disassembly of zinc fingers, thus triggering large-scale unfolding that underlies conversion to the active enzyme. These results suggest that PKC zinc fingers, originally considered purely structural devices, are in fact redox-sensitive flexible hinges, whose conformation is controlled both by redox conditions and lipid agonists.Antioxid. Redox Signal. 14, 757–766.
