title: Membrane targeting: glued by a lipid to the ER.
abstract: Opi1p, a transcription regulator of phospholipid metabolism in budding yeast, is retained in the endoplasmic reticulum by association with Scs2p. New research shows that binding of phosphatidic acid to Opi1p is a prerequisite for this targeting.
authors.affiliation: Institute of Biochemistry, Technical University Graz, Petersgasse 12/2, A-8010 Graz, Austria. guenther.daum@tugraz.at
authors.forename: Günther
authors.initials: G
authors.lastname: Daum
mesh_terms: D004721:Endoplasmic Reticulum / Q000378:metabolism*; D005786:Gene Expression Regulation / Q000502:physiology; D008565:Membrane Proteins / Q000378:metabolism / Q000502:physiology*; D008954:Models, Biological; D010712:Phosphatidic Acids / Q000378:metabolism*; D010743:Phospholipids / Q000378:metabolism*; D012097:Repressor Proteins / Q000378:metabolism*; D029701:Saccharomyces cerevisiae Proteins / Q000378:metabolism*; D015398:Signal Transduction / Q000502:physiology*; D015003:Yeasts
chemical_list: D008565:Membrane Proteins; C096105:OPI1 protein, S cerevisiae; D010712:Phosphatidic Acids; D010743:Phospholipids; D012097:Repressor Proteins; D029701:Saccharomyces cerevisiae Proteins