Further Evidence for Multitopological Localization of Mammalian Porin (VDAC) in the Plasmalemma Forming Part of a Chloride Channel Complex Affected in Cystic Fibrosis and Encephalomyopathy

VDAC/porin is present in sarcoplasmic reticulum from skeletal muscle

“…These sequences are found in the published amino acid sequences of the VDAC1 isoform from bovine brain and of VDAC1/porin 31HL from human B lymphocytes [16].…”

“…4A). Like reconstituted mitochondrial VDAC or VDAC1 (the plasma membrane 31HL porin) [7,9,10,16], the SR channel does not close completely. Inactivation of the reconstituted SR channel by DIDS and DCCD is demonstrated in Fig.…”

“…More recently, however, different studies have demonstrated the expression of mammalian VDAC in different cell compartments other than mitochondria [12][13][14][15][16]. Multiple human porin isoforms have been demonstrated and interpreted as an indication for a variety of functions [17].…”

“…Multiple human porin isoforms have been demonstrated and interpreted as an indication for a variety of functions [17]. Furthermore, VDAC has been shown to be associated with different proteins such as hexokinase, creatine and glycerol kinases, benzodiazepine receptor, adenine nucleotide translocator, the outwardly rectifying depolarization-induced chloride channel (ORDIC) [16,18]. This association is dynamic, constitutes a regulatory interaction and may be involved in several diseases [16,18].…”

The voltage-dependent anion channel-1 modulates apoptotic cell death

“…However, aspartate-glutamate-rich regions including residues Glu87, Asp88 form potential low-affinity Ca 2 þ binding sites, and, based on the proposed VDAC tertiary structure, are predicted to face the pore. 26,27 To identify possible Ca 2 þ binding sites in VDAC and their involvement in VDAC regulation of cell life and death, recombinant murine VDAC (mVDAC)1 or rat VDAC (rVDAC)1, modified by site-directed mutagenesis, were constructed and expressed in Saccharomyces cerevisiae (S. cerevisiae) and U-937 cells. Accordingly, recombinant native and mutated VDAC1 were expressed in the S. cerevisiae strain lacking VDAC1 (M22-2) 28 from which mitochondria were isolated and tested for HK-I binding, and VDACs purified from these mitochondria were tested for their bilayer-reconstituted channel activity.…”