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Vol. 12, Issue 6, 1819-1833, June 2001
*Biochemie-Zentrum Heidelberg (BZH), University of Heidelberg, Im
Neuenheimer Feld 328, 69120 Heidelberg, Germany; and
Sphingomyelin- and cholesterol-enriched microdomains can be
isolated as detergent-resistant membranes from total cell extracts (total-DRM). It is generally believed that this total-DRM represents microdomains of the plasma membrane. Here we describe the purification and detailed characterization of microdomains from Golgi membranes. These Golgi-derived detergent-insoluble complexes (GICs) have a low
buoyant density and are highly enriched in lipids, containing 25% of
total Golgi phospholipids including 67% of Golgi-derived sphingomyelin, and 43% of Golgi-derived cholesterol. In contrast to
total-DRM, GICs contain only 10 major proteins, present in nearly
stoichiometric amounts, including the Max-Planck Institut für Biochemie, Martinsried,
Germany
- and 
-subunits of
heterotrimeric G proteins, flotillin-1, caveolin, and subunits of the
vacuolar ATPase. Morphological data show a brefeldin A-sensitive and
temperature-sensitive localization to the Golgi complex. Strikingly, the stability of GICs does not depend on its membrane environment, because, after addition of brefeldin A to cells, GICs can be isolated from a fused Golgi-endoplasmic reticulum organelle. This indicates that
GIC microdomains are not in a dynamic equilibrium with neighboring membrane proteins and lipids. After disruption of the microdomains by
cholesterol extraction with cyclodextrin, a subcomplex of several GIC
proteins including the B-subunit of the vacuolar ATPase,
flotillin-1, caveolin, and p17 could still be isolated by
immunoprecipitation. This indicates that several of the identified GIC
proteins localize to the same microdomains and that the microdomain
scaffold is not required for protein interactions between these GIC
proteins but instead might modulate their affinity.
Corresponding author. E-mail address:
helms{at}uni-hd.de.
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