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Vol. 9, Issue 1, 191-207, January 1998
Department of Biochemistry, Virginia Polytechnic Institute and
State University, Blacksburg, Virginia 24061-0308
We have addressed the question of whether or not Golgi
fragmentation, as exemplified by that occurring during drug-induced microtubule depolymerization, is accompanied by the separation of Golgi
subcompartments one from another. Scattering kinetics of Golgi
subcompartments during microtubule disassembly and reassembly following
reversible nocodazole exposure was inferred from multimarker analysis
of protein distribution. Stably expressed 
-2,6-sialyltransferase and
N-acetylglucosaminyltransferase-I (NAGT-I), both
C-terminally tagged with the myc epitope, provided markers for the
trans-Golgi/trans-Golgi network (TGN) and
medial-Golgi, respectively, in Vero cells. Using immunogold labeling,
the chimeric proteins were polarized within the Golgi stack. Total
cellular distributions of recombinant proteins were assessed by
immunofluorescence (anti-myc monoclonal antibody) with respect to the
endogenous protein, 
-1,4-galactosyltransferase (GalT,
trans-Golgi/TGN, polyclonal antibody). ERGIC-53 served as a marker for the intermediate compartment). In HeLa cells, distribution of endogenous GalT was compared with transfected rat
-mannosidase II (medial-Golgi, polyclonal antibody). After a 1-h
nocodazole treatment, Vero -2,6-sialyltransferase and GalT were
found in scattered cytoplasmic patches that increased in number over
time. Initially these structures were often negative for NAGT-I, but
over a two- to threefold slower time course, NAGT-I colocalized with
-2,6-sialyltransferase and GalT. Scattered Golgi elements were
located in proximity to ERGIC-53-positive structures. Similar
trans-first scattering kinetics was seen with the HeLa GalT/-mannosidase II pairing. Following nocodazole removal, all cisternal markers accumulated at the same rate in a juxtanuclear Golgi.
Accumulation of cisternal proteins in scattered Golgi elements was not
blocked by microinjected GTP
S at a concentration sufficient to
inhibit secretory processes. Redistribution of Golgi proteins from
endoplasmic reticulum to scattered structures following brefeldin A
removal in the presence of nocodazole was not blocked by GTPS. We
conclude that Golgi subcompartments can separate one from the other. We
discuss how direct trafficking of Golgi proteins from the
TGN/trans-Golgi to endoplasmic reticulum may explain the
observed trans-first scattering of Golgi transferases in
response to microtubule depolymerization.
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