Journal article

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Orm1 and Orm2 are conserved endoplasmic reticulum membrane proteins regulating lipid homeostasis and protein quality control

  • Han, Sumin Department of Molecular, Cellular and Developmental Biology, University of Michigan, Ann Arbor, USA
  • Lone, Museer A. Department of Medicine, Division of Biochemistry, University of Fribourg, Switzerland
  • Schneiter, Roger Department of Medicine, Division of Biochemistry, University of Fribourg, Switzerland
  • Chang, Amy Department of Molecular, Cellular and Developmental Biology, University of Michigan, Ann Arbor, USA
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    2010
Published in:
  • Proceedings of the National Academy of Sciences. - 2010
English Yeast members of the ORMDL family of endoplasmic reticulum (ER) membrane proteins play a central role in lipid homeostasis and protein quality control. In the absence of yeast Orm1 and Orm2, accumulation of long chain base, a sphingolipid precursor, suggests dysregulation of sphingolipid synthesis. Physical interaction between Orm1 and Orm2 and serine palmitoyltransferase, responsible for the first committed step in sphingolipid synthesis, further supports a role for the Orm proteins in regulating sphingolipid synthesis. Phospholipid homeostasis is also affected in orm1∆ orm2∆ cells: the cells are inositol auxotrophs with impaired transcriptional regulation of genes encoding phospholipid biosynthesis enzymes. Strikingly, impaired growth of orm1∆ orm2∆ cells is associated with constitutive unfolded protein response, sensitivity to stress, and slow ER-to-Golgi transport. Inhibition of sphingolipid synthesis suppresses orm1∆ orm2∆ phenotypes, including ER stress, suggesting that disrupted sphingolipid homeostasis accounts for pleiotropic phenotypes. Thus, the yeast Orm proteins control membrane biogenesis by coordinating lipid homeostasis with protein quality control.
Faculty
Faculté des sciences et de médecine
Department
Département de Biologie
Language
  • English
Classification
Biology
License
License undefined
Identifiers
Persistent URL
https://folia.unifr.ch/unifr/documents/301433
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