Identification of Triton X-100 insoluble membrane domains in the yeast Saccharomyces cerevisiae. Lipid requirements for targeting of heterotrimeric G-protein subunits.

The Journal of Biological Chemistry
E KüblerM P Lisanti

Abstract

Low density Triton X-100 insoluble (LDTI) membrane domains are found in most mammalian cell types. Previous biochemical and immunolocalization studies have revealed the presence of G-protein coupled receptors and heterotrimeric G-protein subunits (Galpha and Gbetagamma subunits) within these structures, implicating mammalian LDTI membrane domains in G-protein coupled signaling. Here, we present biochemical evidence that similar LDTI structures exist in a genetically tractable organism, the yeast Saccharomyces cerevisiae. Yeast LDTI membranes were purified based on the known biochemical properties of mammalian LDTI membranes: (i) their Triton X-100 insolubility; and (ii) their discrete buoyant density in sucrose gradients. As with purified mammalian LDTI membranes, these yeast LDTI membranes harbor the subunits of the heterotrimeric G-proteins (Galpha and Gbetagamma subunits). Other plasma membrane marker proteins (the plasma membrane H+-ATPase and a GPI-linked protein Gas1p) are preferentially excluded from these purified fractions. Mutational and genetic analyses were performed to define the requirements for the targeting of G-protein subunits to these yeast membrane domains. We find that the targeting of Galpha is independent...Continue Reading

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