VDAC proteomics: Post-translation modifications

Voltage-dependent anion channels are abundant mitochondrial outer membrane proteins expressed in three isoforms, VDAC1-3, and are considered as “mitochondrial gatekeepers”. 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.

► Phosphorylation of VDAC on serine, threonine, and tyrosine has been detected.
► Phosphorylation of serine 12 and 103 decreases degradation of VDAC1 that is associated with increased apoptosis.
► Phosphorylation of serine 193 prevents cell death.
► Lysine acetylation has been detected but functional consequences have not been studied.