Post-translational modifications of rat liver mitochondrial outer membrane proteins identified by mass spectrometry
Post-translational modifications of rat liver mitochondrial outer membrane proteins identified by mass spectrometry
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DOI：
10.1016/j.bbapap.2007.03.012
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发表时间：
2007-05-01
影响因子：
3.2
通讯作者：
Hoppel, Charles L.
中科院分区：
文献类型：
--
作者：
Distler, Anne M.;Kerner, Janos;Hoppel, Charles L.
翻译后修饰的鉴定是困难的，尤其是对于疏水性膜蛋白。在这里，我们提出了几种类型的蛋白质修饰的线粒体外膜分离的膜蛋白的鉴定。我们表明，在体内，成熟的大鼠肝脏线粒体肉毒碱棕榈酰转移酶-I酶的N-末端乙酰化，磷酸化的两个苏氨酸残基，和硝化的两个酪氨酸残基。我们发现，长链酰基辅酶A合成酶I是乙酰化的N-末端和赖氨酸残基和酪氨酸残基被磷酸化和硝化。对于线粒体中存在的三种电压依赖性阴离子通道亚型，确定了蛋白质的N-末端区域，并鉴定了磷酸化位点。这些新的发现提出了关于肉毒碱棕榈酰转移酶-I，长链酰基辅酶A合成酶和电压依赖性阴离子通道的调控方面的问题，进一步的研究应该推进我们对线粒体脂肪酸氧化的调控的理解，一般和这三种蛋白质的具体。(C)2007 Elsevier B. V.保留所有权利。
The identification of post-translational modifications is difficult especially for hydrophobic membrane proteins. Here we present the identification of several types of protein modifications on membrane proteins isolated from mitochondrial outer membranes. We show, in vivo, that the mature rat liver mitochondrial carnitine palmitoyltransferase-I enzyme is N-terminally acetylated, phosphorylated on two threonine residues, and nitrated on two tyrosine residues. We show that long chain acyl-CoA synthetase I is acetylated at both the N-terminal end and at a lysine residue and tyrosine residues are found to be phosphorylated and nitrated. For the three voltage-dependent anion channel isoforms present in the mitochondria, the N-terminal regions of the protein were determined and sites of phosphorylation were identified. These novel findings raise questions about regulatory aspects of carnitine palmitoyltransferase-I, long chain acyl-CoA synthetase and voltage dependent anion channel and further studies should advance our understanding about regulation of mitochondrial fatty acid oxidation in general and these three proteins in specific. (C) 2007 Elsevier B.V. All rights reserved.