TAILIEUCHUNG - Báo cáo khoa học: Subcellular localization of yeast Sec14 homologues and their involvement in regulation of phospholipid turnover

Sec14p of the yeastSaccharomyces cerevisiaeis involved in protein secretion and regulation of lipid synthesis and turnover in vivo, but acts as a phosphatidylinositol–phos-phatidylcholine transfer proteinin vitro. In this work, the five homologues of Sec14p, Sfh1p–Sfh5p, were subjected to biochemical andcell biological analysis toget abetter viewof their physiological role. We show that overexpression of SFH2andSFH4suppressed thesec14growth defect in a more andSFH1in a less efficient way, whereas overexpres-sion ofSFH3andSFH5did not complementsec14 | Eur. J. Biochem. 270 3133-3145 2003 FEBS 2003 doi Subcellular localization of yeast Sec14 homologues and their involvement in regulation of phospholipid turnover Martina Schnabl1 Olaa V Oskolkova1 Roman Holic2 Barbara Brezna2 Harald Pichler3 Milos ZaaorSek2 . Sepp D. Kohlwein4 Fritz Paltauf1 Gunther Daum1 and Peter GriaC2 1 Department of Biochemistry University of Technology Graz Austria 2Institute of Animal Biochemistry and Genetics Slovak Academy of Sciences Ivanka pri Dunaji Slovak Republic 3Department of Biochemistry Faculty of Sciences Sciences II University of Geneva Switzerland 4Department of Molecular Biology Biochemistry and Microbiology SFB Biomembrane Research Center University of Graz Austria Sec14p of the yeast Saccharomyces cerevisiae is involved in protein secretion and regulation of lipid synthesis and turnover in vivo but acts as a phosphatidylinositol-phos-phatidylcholine transfer protein in vitro. In this work the five homologues of Sec14p Sfh1p-Sfh5p were subjected to biochemical and cell biological analysis to get a better view of their physiological role. We show that overexpression of SFH2 and SFH4 suppressed the sec14 growth defect in a more and SFH1 in a less efficient way whereas overexpression of SFH3 and SFH5 did not complement sec14. Using C-terminal yEGFP fusions Sfh2p Sfh4p and Sfh5p are mainly localized to the cytosol and microsomes similar to Sec14p. Sfh1p was detected in the nucleus and Sfh3p in lipid particles and in microsomes. In contrast to Sec14p which inhibits phospholipase D1 Pld1p overproduction of Sfh2p and Sfh4p resulted in the activation of Pld1p-mediated phosphatidylcholine turnover. Interestingly Sec14p and the two homologues Sfh2p and Sfh4p downregulate phospholipase B1 Plb1p -mediated turnover of phosphatidylcholine in vivo. In summary Sfh2p and Sfh4p are the Sec14p homologues with the most pronounced functional similarity to Sec14p whereas the other Sfh proteins appear to be .

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