| First Author | Naghdi S | Year | 2016 |
| Journal | Biochim Biophys Acta | Volume | 1863 |
| Issue | 10 | Pages | 2503-14 |
| PubMed ID | 27116927 | Mgi Jnum | J:255627 |
| Mgi Id | MGI:6105075 | Doi | 10.1016/j.bbamcr.2016.04.020 |
| Citation | Naghdi S, et al. (2016) VDAC2-specific cellular functions and the underlying structure. Biochim Biophys Acta 1863(10):2503-14 |
| abstractText | Voltage Dependent Anion-selective Channel 2 (VDAC2) contributes to oxidative metabolism by sharing a role in solute transport across the outer mitochondrial membrane (OMM) with other isoforms of the VDAC family, VDAC1 and VDAC3. Recent studies revealed that VDAC2 also has a distinctive role in mediating sarcoplasmic reticulum to mitochondria local Ca(2+) transport at least in cardiomyocytes, which is unlikely to be explained simply by the expression level of VDAC2. Furthermore, a strictly isoform-dependent VDAC2 function was revealed in the mitochondrial import and OMM-permeabilizing function of pro-apoptotic Bcl-2 family proteins, primarily Bak in many cell types. In addition, emerging evidence indicates a variety of other isoform-specific engagements for VDAC2. Since VDAC isoforms display 75% sequence similarity, the distinctive structure underlying VDAC2-specific functions is an intriguing problem. In this paper we summarize studies of VDAC2 structure and functions, which suggest a fundamental and exclusive role for VDAC2 in health and disease. This article is part of a Special Issue entitled: Mitochondrial Channels edited by Pierre Sonveaux, Pierre Maechler and Jean-Claude Martinou. |
