VDAC proteomics: Post-translation modifications

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• 作者：Janos Kerner^a ; ^b ; Kwangwon Lee^a ; ^b ; Bernard Tandler^a ; ^d ; Charles L. Hoppel^a ; ^b ; ^c ; ^{charles.hoppel@case.edu}
• 关键词：Mitochondrial outer membrane ; Acetyl-lysine ; Phosphorylation
• 刊名：Biochimica et Biophysica Acta (BBA)/Biomembranes
• 出版年：2012
• 期刊代码：14_00052736
• 类别：bio
• 出版时间：June, 2012
• 卷：1818
• 期：6
• 页码：1520-1525
• 文件大小：189 K

摘要

Voltage-dependent anion channels are abundant mitochondrial outer membrane proteins expressed in three isoforms, VDAC1-3, and are considered as 鈥渕itochondrial gatekeepers鈥? Most tissues express all three isoforms. The functions of VDACs are several-fold, ranging from metabolite and energy exchange to apoptosis. Some of these functions depend on or are affected by interaction with other proteins in the cytosol and intermembrane space. Furthermore, the function of VDACs, as well as their interaction with other proteins, is affected by posttranslational modification, mainly phosphorylation. This review summarizes recent findings on posttranslational modification of VDACs and discusses the physiological outcome of these modifications. This article is part of a Special Issue entitled: VDAC structure, function, and regulation of mitochondrial metabolism.