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J Biol Chem, Vol. 273, Issue 45, 29565-29576, November 6, 1998
From the Department of Molecular Biology, Princeton University,
Princeton, New Jersey 08544
Intracellular protein traffic involves a tightly
regulated series of events in which a membrane-bounded vesicles bud
from one compartment and are specifically targeted to the next
compartment, where they dock and fuse. A cell-free system that
reconstitutes vesicle trafficking between the cis and
medial Golgi cisternae has been used previously to identify several
proteins involved in vesicular transport
(N-ethylmaleimide-sensitive fusion protein, soluble N-ethylmaleimide-sensitive fusion
protein attachment proteins, p115, and p16); however, these factors are
insufficient to drive the transport reaction. We have used a modified
version of this in vitro intra-Golgi transport assay to
guide purification of a new transport-stimulating activity. The active
component is a 13 S hetero-oligomeric complex consisting of at least
five polypeptides (approximately 110, 109, 90, 82, and 71 kDa), which
we term Golgi transport complex (GTC). Hydrodynamic properties suggest
that GTC is approximately 800 kDa and nonglobular. We obtained peptide sequence information from the 90-kDa subunit (GTC-90) that allowed us
to identify a number of GTC-90 cDNAs. Comparison of these cDNAs with one another and with the genomic sequence suggests that the GTC-90
mRNA is alternatively spliced. Anti-GTC-90 antibodies inhibit the
in vitro Golgi transport assay, confirming the
functionality of the purified complex. Subcellular fractionation
indicates that GTC-90 exists in both membrane and cytosolic pools, with
the cytosolic pool associated exclusively with the GTC complex. The
membrane-associated pool of GTC-90 is localized to the Golgi apparatus.
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