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The voltage-dependent anion channel of the outer mitochondrial
membrane, VDAC (also known as mitochondrial porin), is a small abundant
protein which forms a voltage-gated pore when incorporated into planar
lipid bilayers. This protein forms the primary pathway for movement of
major metabolites through the outer membrane. Recently, it has been
demonstrated that two human VDAC genes, HVDAC1 and HVDAC2, produce
three proteins that differ most significantly at their amino termini.
These results suggest that the distinct amino termini lead to the
targeting of individual VDAC isoforms to different cellular
compartments. Consistent with this hypothesis, recent reports suggest
that HVDAC1 is found in the plasma membrane of mammalian cells. To
define the subcellular location of HVDAC isoforms, HVDAC genes were
modified so that the encoded proteins contain COOH-terminal epitopes
recognized by either of two monoclonal antibodies. Introduction of
these epitope tags had no effect on the function of modified VDAC
proteins. Epitope-tagged proteins were then individually expressed in
COS7 cells or rat astrocytes and the intracellular location of each
isoform subsequently identified by subcellular fractionation, light
level immunofluorescence, and immunoelectron microscopy. Our results
demonstrate that each HVDAC protein is exclusively located in fractions
or subcellular regions containing mitochondrial marker proteins. In
addition, immunofluorescence and immunoelectron microscopy show that an
individual mitochondrion can contain both HVDAC1 and HVDAC2. Our
results call into question previous reports demonstrating VDAC
molecules in the plasma membrane and suggest that functional
differences between individual VDAC isoforms may result in distinct
regulatory processes within a single mitochondrion.
Volume 270,
Number 23,
Issue of June 9, pp. 13998-14006, 1995
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
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