The Golgi apparatus in animal cells comprises a reticulum of linked stacks
in the pericentriolar and often in the juxtanuclear regions of the cell(1).
The unique architecture of this organelle is thought to depend on the cyto
skeleton(2) and cytoplasmic matrix proteins(3,4)-the best characterized bei
ng the golgin family of fibrous, coiled-coil proteins and the GRASP family
of stacking proteins(5-10). Here we show that these matrix proteins can be
separated from oligosaccharide-modifying enzymes in the Golgi stack without
affecting their ability to form a ribbon-like reticulum in the correct loc
ation near to the nucleus. Our data suggest that the Golgi is a structural
scaffold that can exist independently of, but is normally populated by, the
enzyme-containing membranes that modify transiting cargo. This new concept
of the Golgi further indicates that the Golgi may be an autonomous organel
le rather than one that is in simple dynamic equilibrium with the endoplasm
ic reticulum.