Journal article

Acyl-CoA-binding protein, Acb1p, is required for normal vacuole function and ceramide synthesis in Saccharomyces cerevisiae

  • Faergeman, Nils J. Department of Biochemistry and Molecular Biology, University of Southern Denmark, Odense M, Denmark
  • Feddersen, Søren Department of Biochemistry and Molecular Biology, University of Southern Denmark, Odense M, Denmark
  • Christiansen, Janne K. Department of Biochemistry and Molecular Biology, University of Southern Denmark, Odense M, Denmark
  • Larsen, Morten K. Department of Biochemistry and Molecular Biology, University of Southern Denmark, Odense M, Denmark
  • Schneiter, Roger Division of Biochemistry, Department of Medicine, University of Fribourg, Switzerland
  • Ungermann, Christian Biochemie-Zentrum Heidelberg, Germany
  • Mutenda, Kudzai Department of Biochemistry and Molecular Biology, University of Southern Denmark, Odense M, Denmark
  • Roepstroff, Peter Department of Biochemistry and Molecular Biology, University of Southern Denmark, Odense M, Denmark
  • Knudsen, Jens Department of Biochemistry and Molecular Biology, University of Southern Denmark, Odense M, Denmark
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    19.04.2004
Published in:
  • Biochemical Journal. - 2004, vol. 380, no. 907-918
English In the present study, we show that depletion of acyl-CoA-binding protein, Acb1p, in yeast affects ceramide levels, protein trafficking, vacuole fusion and structure. Vacuoles in Acb1p-depleted cells are multi-lobed, contain significantly less of the SNAREs (soluble N-ethylmaleimide-sensitive fusion protein attachment protein receptors) Nyv1p, Vam3p and Vti1p, and are unable to fuse in vitro. Mass spectrometric analysis revealed a dramatic reduction in the content of ceramides in whole-cell lipids and in vacuoles isolated from Acb1p-depleted cells. Maturation of yeast aminopeptidase I and carboxypeptidase Y is slightly delayed in Acb1p-depleted cells, whereas the maturation of alkaline phosphatase and Gas1p is unaffected. The fact that Gas1p maturation is unaffected by Acb1p depletion, despite the lowered ceramide content in these cells, indicates that ceramide synthesis in yeast could be compartmentalized. We suggest that the reduced ceramide synthesis in Acb1p-depleted cells leads to severely altered vacuole morphology, perturbed vacuole assembly and strong inhibition of homotypic vacuole fusion.
Faculty
Faculté des sciences et de médecine
Department
Département de Biologie
Language
  • English
Classification
Medicine
License
License undefined
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Persistent URL
https://folia.unifr.ch/unifr/documents/299779
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