1.B.8.1.12
Mitochondrial outer membrane voltage-dependent anion-selective channel protein 2, VDAC-2 of 294 aas.  Protein:micelle ratios and cysteine residues in the protein influence VDAC2 stability and unfolding rates (Maurya and Mahalakshmi 2014).  VDAC-2  performs a different subset of regulatory functions than VDAC1. It has anti-apoptotic features and contributes to gametogenesis.It may also regulate ROS, steroidogenesis and mitochondria-associated endoplasmic reticulum membrane regulatory pathways (Maurya and Mahalakshmi 2015).  Plays a role in mitochondrial import of Bak and tBid-induced apoptosis (Naghdi et al. 2015). VDAC2 plasticity and stability in the mitochondrial outer membrane are modulated by physical properties of the bilayer (Srivastava et al. 2018). VDAC1 and VDAC2 are overall, very similar, exhibiting similar dynamic behavior and conformational homogeneity (Eddy et al. 2019). Altered skeletal muscle microtubule-mitochondrial VDAC2 binding is related to bioenergetic impairments after paclitaxel but not vinblastine chemotherapies (Ramos et al. 2019). Intramolecular disulfide bridges are present in VDAC2 from Rattus norvegicus (Pittalà et al. 2024).  Voltage-dependent anion channel 2 (VDAC2) plays a crucial role in the host response to viral infection. The receptor for activated C kinase 1 (RACK1) is also a key host factor involved in viral replication.