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Vol. 11, Issue 7, 2267-2281, July 2000
Medical Research Council Laboratory of Molecular Biology, Cambridge
CB2 2QH, United Kingdom
The plasma membrane of eukaryotic cells differs in lipid
composition from most of the internal organelles, presumably reflecting differences in many of its functions. In particular, the plasma membrane is rich in sphingolipids and sterols, one property of which is
to decrease the permeability and increase the thickness of lipid
bilayers. In this paper, we examine the length of transmembrane domains
throughout the yeast secretory pathway. Although the transmembrane domains of cis and medial Golgi residents
are similar to those of endoplasmic reticulum proteins, these domains
lengthen substantially beyond the medial Golgi,
suggesting a thickening of the bilayer. Yeast sphingolipids have
particularly long acyl chains, and Aur1p, the inositol
phosphorylceramide synthase that initiates yeast sphingolipid
synthesis, was found to be located in the Golgi apparatus by both
immunofluorescence and membrane fractionation, with its active site
apparently in the Golgi lumen. Thus, it appears that sphingolipid
synthesis in yeast takes place in the Golgi, separated from
glycerophospholipid synthesis in the endoplasmic reticulum. A similar
separation has been found in mammalian cells, and this conservation
suggests that such an arrangement of enzymes within the secretory
pathway could be important for the creation of bilayers of different
thickness within the cell.
Corresponding author. E-mail address:
sean{at}mrc-lmb.cam.ac.uk.
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