Evidence for secretory pathway localization of a voltage-dependent anion channel isoform.

Abstract:

:Voltage-dependent anion channels (VDACs) are pore-forming proteins (porins) that form the major pathway for movement of adenine nucleotides through the outer mitochondrial membrane. Electrophysiological studies indicate that VDAC-like channel activity is also prevalent in the cell membranes of many mammalian cells. However, the multitopological localization of porins outside the mitochondrion has remained an extremely controversial issue. Herein, we show that usage of two alternative first exons of the murine VDAC-1 gene leads to expression of two porins differing within their N termini. One porin (plasmalemmal VDAC-1) harboring a hydrophobic leader peptide is primarily targeted through the Golgi apparatus to the cell membrane. In contrast, the second isoform lacking the N-terminal leader (mitochondrial VDAC-1) is translocated more efficiently into the outer mitochondrial membrane. Thus, our data provide unique genetic evidence in favor of a multitopological localization of a mitochondrial porin.

authors

Buettner R,Papoutsoglou G,Scemes E,Spray DC,Dermietzel R

doi

10.1073/pnas.060242297

keywords:

subject

Has Abstract

pub_date

2000-03-28 00:00:00

pages

3201-6

issue

7

eissn

0027-8424

issn

1091-6490

pii

060242297

journal_volume

97

pub_type

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