Salvi Mauro, Morrice Nick A, Brunati Anna Maria, Toninello Antonio
Department of Biological Chemistry, University of Padova, Viale G Colombo 3, 35121, Padova, Italy.
FEBS Lett. 2007 Dec 11;581(29):5579-85. doi: 10.1016/j.febslet.2007.11.005. Epub 2007 Nov 13.
Overlooked until recently, mitochondrial protein phosphorylation is now emerging as a key post-translational mechanism in the regulation of mitochondrial functions. In particular, tyrosine phosphorylation represents a promising field to discover new mechanisms of bioenergetic regulation. Tyrosine kinases belonging to the Src kinase family have been observed in mitochondrial compartments, however their substrates are almost unknown. Here, we provide evidence that the flavoprotein of succinate dehydrogenase and aconitase are "in vitro" substrates of Fgr tyrosine kinase. Fgr phosphorylates flavoprotein of succinate dehydrogenase at Y535 and Y596 and aconitase at Y71, Y544 and Y665. The significance of these findings is discussed.
线粒体蛋白磷酸化直到最近才被人们所忽视，现在它正作为一种关键的翻译后机制在调节线粒体功能中崭露头角。特别是，酪氨酸磷酸化是发现生物能量调节新机制的一个很有前景的领域。属于Src激酶家族的酪氨酸激酶已在线粒体区室中被观察到，然而其底物几乎未知。在此，我们提供证据表明，琥珀酸脱氢酶黄素蛋白和乌头酸酶是Fgr酪氨酸激酶的“体外”底物。Fgr在Y535和Y596位点磷酸化琥珀酸脱氢酶黄素蛋白，在Y71、Y544和Y665位点磷酸化乌头酸酶。本文讨论了这些发现的意义。
