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Vol. 9, Issue 7, 1649-1660, July 1998
Division of Human Immunology, Hanson Centre for Cancer Research,
Adelaide 5000, South Australia, Australia
Screening of a library derived from primary human endothelial cells
revealed a novel human isoform of vesicle-associated membrane protein-1
(VAMP-1), a protein involved in the targeting and/or fusion of
transport vesicles to their target membrane. We have termed this novel
isoform VAMP-1B and designated the previously described isoform
VAMP-1A. VAMP-1B appears to be an alternatively spliced form of VAMP-1.
A similar rat splice variant of VAMP-1 (also termed VAMP-1B) has
recently been reported. Five different cultured cell lines, from
different lineages, all contained VAMP-1B but little or no detectable
VAMP-1A mRNA, as assessed by PCR. In contrast, brain mRNA contained
VAMP-1A but no VAMP-1B. The VAMP-1B sequence encodes a protein
identical to VAMP-1A except for the carboxy-terminal five amino acids.
VAMP-1 is anchored in the vesicle membrane by a carboxy-terminal
hydrophobic sequence. In VAMP-1A the hydrophobic anchor is followed by
a single threonine, which is the carboxy-terminal amino acid. In
VAMP-1B the predicted hydrophobic membrane anchor is shortened by four
amino acids, and the hydrophobic sequence is immediately followed by
three charged amino acids, arginine-arginine-aspartic acid.
Transfection of human endothelial cells with epitope-tagged VAMP-1B
demonstrated that VAMP-1B was targeted to mitochondria whereas VAMP-1A
was localized to the plasma membrane and endosome-like structures. Analysis of C-terminal mutations of VAMP-1B demonstrated that mitochondrial targeting depends both on the addition of positive charge
at the C terminus and a shortened hydrophobic membrane anchor. These
data suggest that mitochondria may be integrated, at least at a
mechanistic level, to the vesicular trafficking pathways that govern
protein movement between other organelles of the cell.
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