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.
journal_name
Proc Natl Acad Sci U S Aauthors
Buettner R,Papoutsoglou G,Scemes E,Spray DC,Dermietzel Rdoi
10.1073/pnas.060242297keywords:
subject
Has Abstractpub_date
2000-03-28 00:00:00pages
3201-6issue
7eissn
0027-8424issn
1091-6490pii
060242297journal_volume
97pub_type
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