Glycosylphosphatidylinositol-anchored Proteins Are Required for the Transport of Detergent-resistant Microdomain-associated Membrane Proteins Tat2p and Fur4p

In eukaryotic cells many cell surface proteins are attached to the membrane via the glycosylphosphatidylinositol (GPI) moiety. In yeast, GPI also plays important roles in the production of mannoprotein in the cell wall. We previously isolated gwt1 mutants and found that GWT1 is required for inositol acylation in the GPI biosynthetic pathway. In this study we isolated a new gwt1 mutant allele, gwt1-10, that shows not only high temperature sensitivity but also low temperature sensitivity. The gwt1-10 cells show impaired acyltransferase activity and attachment of GPI to proteins even at the permissive temperature. We identified TAT2, which encodes a high affinity tryptophan permease, as a multicopy suppressor of cold sensitivity in gwt1-10 cells. The gwt1-10 cells were also defective in the import of tryptophan, and a lack of tryptophan caused low temperature sensitivity. Microscopic observation revealed that Tat2p is not transported to the plasma membrane but is retained in the endoplasmic reticulum in gwt1-10 cells grown under tryptophan-poor conditions. We found that Tat2p was not associated with detergent-resistant membranes (DRMs), which are required for the recruitment of Tat2p to the plasma membrane. A similar result was obtained for Fur4p, a uracil permease localized in the DRMs of the plasma membrane. These results indicate that GPI-anchored proteins are required for the recruitment of membrane proteins Tat2p and Fur4p to the plasma membrane via DRMs, suggesting that some membrane proteins are redistributed in the cell in response to environmental and nutritional conditions due to an association with DRMs that is dependent on GPI-anchored proteins. In eukaryotic cells many cell surface proteins are attached to the membrane via the glycosylphosphatidylinositol (GPI) moiety. In yeast, GPI also plays important roles in the production of mannoprotein in the cell wall. We previously isolated gwt1 mutants and found that GWT1 is required for inositol acylation in the GPI biosynthetic pathway. In this study we isolated a new gwt1 mutant allele, gwt1-10, that shows not only high temperature sensitivity but also low temperature sensitivity. The gwt1-10 cells show impaired acyltransferase activity and attachment of GPI to proteins even at the permissive temperature. We identified TAT2, which encodes a high affinity tryptophan permease, as a multicopy suppressor of cold sensitivity in gwt1-10 cells. The gwt1-10 cells were also defective in the import of tryptophan, and a lack of tryptophan caused low temperature sensitivity. Microscopic observation revealed that Tat2p is not transported to the plasma membrane but is retained in the endoplasmic reticulum in gwt1-10 cells grown under tryptophan-poor conditions. We found that Tat2p was not associated with detergent-resistant membranes (DRMs), which are required for the recruitment of Tat2p to the plasma membrane. A similar result was obtained for Fur4p, a uracil permease localized in the DRMs of the plasma membrane. These results indicate that GPI-anchored proteins are required for the recruitment of membrane proteins Tat2p and Fur4p to the plasma membrane via DRMs, suggesting that some membrane proteins are redistributed in the cell in response to environmental and nutritional conditions due to an association with DRMs that is dependent on GPI-anchored proteins. Glycosylphosphatidylinositol (GPI) 3The abbreviations used are: GPI, glycosylphosphatidylinositol; PI, phosphatidylinositol; GlcN-(acyl)PI, glucosaminyl(acyl)-PI; ER, endoplasmic reticulum; CoA, coenzyme A; DRMs, detergent-resistant membranes; TX-100, Triton X-100; CHAPS, 3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulfonate; SC, synthetic complete; mRFP, monomeric red fluorescent protein; GFP, green fluorescent protein; HA, hemagglutinin; ConA, concanavalin A; Ts–, high temperature sensitivity; Cs–, cold sensitivity; 5-FU, 5-fluorouracil. anchoring is a mechanism by which proteins are attached to the cell surface in all eukaryotic cells (1.Englund P.T. Annu. Rev. Biochem. 1993; 62: 121-138Crossref PubMed Google Scholar, 2.McConville M.J. Ferguson M.A. Biochem. J. 1993; 294: 305-324Crossref PubMed Scopus (810) Google Scholar). GPI-anchored proteins have various physiological roles contributing to transmembrane signaling, cell surface protection, cell adhesion, and cell wall synthesis (3.Lisanti M.P. Rodriguez-Boulan E. Saltiel A.R. J. Membr. Biol. 1990; 117: 1-10Crossref PubMed Scopus (82) Google Scholar, 4.Klis F.M. Yeast. 1994; 10: 851-869Crossref PubMed Scopus (492) Google Scholar). In yeast, GPI-anchored proteins are major components of the cell wall, and they are essential for cell wall integrity (5.Kapteyn J.C. Van Den Ende H. Klis F.M. PubMed Scopus Google Scholar, J. Biol. PubMed Scopus Google and cell J. Biol. 1994; PubMed Google Scholar, J. Biol. PubMed Scopus Google Scholar, H. J. Biol. PubMed Scopus Google Scholar). The GPI is in the endoplasmic reticulum is to the of proteins a GPI attachment The GPI a M.J. Ferguson M.A. Biochem. J. 1993; 294: 305-324Crossref PubMed Scopus (810) Google Scholar, J. Biol. PubMed Google which by the of an to the inositol and a to the Ferguson M.A. PubMed Scopus Google Scholar, J. Biol. PubMed Google Scholar, E. J. Biol. PubMed Google Scholar, J. Biol. PubMed Google Scholar). The of the GPI is also to as of the attachment M.J. Ferguson M.A. Biochem. J. 1993; 294: 305-324Crossref PubMed Scopus (810) Google Scholar). In and inositol is the in the GPI biosynthetic We previously that is required for this in J. Biol. PubMed Scopus Google Scholar). In cells a is to by and acylation of inositol is for the attachment of GPI to proteins H. Biol. PubMed Scopus Google Scholar). In GPI-anchored proteins are in and PubMed Scopus Google Scholar, E. PubMed Scopus Google Scholar). A of is to with Triton they are to as detergent-resistant membranes proteins are to but to as 1993; PubMed Scopus Google Scholar). These and also to as roles in and membrane PubMed Scopus Google Scholar, J. Biol. PubMed Scopus Google Scholar, J. Biol. PubMed Scopus Google Scholar, PubMed Scopus Google Scholar, Rev. Biol. PubMed Scopus Google Scholar, Biol. PubMed Scopus Google Scholar). In DRMs are of and which is and they GPI-anchored proteins similar to found in cells PubMed Scopus Google Scholar, E. PubMed Scopus Google Scholar). the physiological of GPI-anchored proteins in DRMs of cells are are to a GPI-anchored the to the plasma membrane PubMed Scopus Google Scholar). The results obtained in in which is in a that the of DRMs and association with GPI-anchored are in the PubMed Scopus Google Scholar, PubMed Scopus Google Scholar). as GPI-anchored proteins with DRMs in the of PubMed Scopus Google and is required for the of GPI-anchored proteins the to the H. J. 1994; PubMed Scopus Google Scholar, H. J. PubMed Google Scholar, H. J. Biol. PubMed Scopus Google Scholar). the of GPI-anchored proteins that are to the GPI-anchored proteins by in the of in the GPI-anchored many plasma membrane as Fur4p, and have to associated with DRMs, which are required for the of proteins to the plasma membrane PubMed Scopus Google Scholar, PubMed Scopus Google Scholar, J. Biol. PubMed Scopus Google Scholar, J. Biol. PubMed Scopus Google Scholar, J. Biol. PubMed Scopus Google Scholar). Tat2p is a high affinity tryptophan permease is by the tryptophan high tryptophan Tat2p membrane proteins are to the and to the the at low tryptophan they are to the plasma membrane J. Biol. PubMed Scopus Google Scholar). In which are defective in the synthesis of Tat2p with DRMs and is and to the even at low tryptophan J. Biol. PubMed Scopus Google Scholar). 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