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J Biol Chem, Vol. 273, Issue 30, 19030-19039, July 24, 1998
From the Imperial Cancer Research Fund, Cell Biology Laboratory,
44 Lincoln's Inn Fields,
London WC2A 3PX, United Kingdom
We have used isolated rat liver Golgi membranes
to reconstitute the synthesis of sulfated glycosaminoglycans (GAGs)
onto the membrane-permeable, external acceptor xyloside. Biosynthetic
labeling of GAGs with [35S]sulfate in
vitro is shown to have an absolute requirement for ATP and
cytosolic proteins and is inhibited by dismantling the Golgi apparatus
with okadaic acid or under mitotic conditions suggesting that
inter-compartmental transport between Golgi cisternae is a prerequisite
for the successful completion of the initiation, polymerization, and
sulfation of GAGs. Accordingly, we show that in vitro
synthesis of 35S-GAGs utilizes the same machinery employed
in Golgi transport events in terms of vesicle budding (ADP-ribosylation
factor and coatomer), docking (Rabs), targeting (SNAREs), and fusion
(N-ethylmaleimide-sensitive factor). This provides
compelling evidence that GAGs synthesis is linked to Golgi membrane
traffic and suggests that it can be used as a
complementation-independent method to study membrane transport in Golgi
preparations from any source. We have applied this system to show that
intra-Golgi traffic requires the function of the Golgi target-SNARE,
syntaxin 5.
In Vitro Synthesis of Sulfated Glycosaminoglycans
Coupled to Inter-compartmental Golgi Transport
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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