Reconstitution of yeast microsomal lipid flip-flop using endogenous aminophospholipids

Research output: Contribution to journalArticle

19 Citations (Scopus)

Abstract

The molecular basis of transbilayer movement or flipping of phospholipids in the endoplasmic reticulum is largely unknown. To circumvent the problems inherent to studies with artificial phospholipid analogs, we studied microsomal flip-flop of endogenous phosphatidylethanolamine in yeast. The transbilayer transport of phosphatidylethanolamine was measured in reconstituted proteoliposomes derived from microsomal detergent extracts. Our results demonstrate that flipping is protease sensitive but does not require metabolic energy. Our assay is the first to use the endogenous substrate of the so-called 'flippase' to study phospholipid translocation in endomembranes and may therefore be crucial for the understanding of the catalytic properties of this elusive enzyme. Copyright (C) 2000 Federation of European Biochemical Societies.

Original languageEnglish (US)
Pages (from-to)277-281
Number of pages5
JournalFEBS Letters
Volume476
Issue number3
DOIs
StatePublished - Jul 7 2000
Externally publishedYes

Fingerprint

Flip flop circuits
Yeast
Phospholipids
Yeasts
Lipids
Endoplasmic Reticulum
Detergents
Assays
Peptide Hydrolases
Substrates
Enzymes
phosphatidylethanolamine

Keywords

  • Membrane biogenesis
  • Phosphatidylethanolamine
  • Phospholipid flip-flop
  • Saccharomyces cerevisiae

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Reconstitution of yeast microsomal lipid flip-flop using endogenous aminophospholipids. / Nicolson, Teresa; Mayinger, Peter.

In: FEBS Letters, Vol. 476, No. 3, 07.07.2000, p. 277-281.

Research output: Contribution to journalArticle

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