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Role of ATP and disulphide bonds during protein folding in the endoplasmic reticulum

Nature volume 356, pages 260262 (19 March 1992) | Download Citation

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Abstract

BEING topologically equivalent to the extracellular space, the lumen of the endoplasmic reticulum (ER) provides a unique folding environment for newly synthesized proteins. Unlike other compartments in the cell where folding occurs, the ER is oxidizing and therefore can promote the formation of disulphide bonds1. The reducing agent dithiothreitol, when added to living cells, inhibits disulphide formation with profound effects on folding2. Taking advantage of this effect, we demonstrate here that folding of influenza haemagglutinin is energy dependent. Metabolic energy is required to support the correct folding and disulphide bond formation in this well characterized viral glycoprotein, to rescue misfolded proteins from disulphide-linked aggregates, and to maintain the oxidized protein in its folded and oligomerization-competent state.

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  1. Department of Cell Biology, Yale University School of Medicine, 333 Cedar Street, New Haven, Connecticut 06510-8002, USA

    • Ineke Braakman
    • , Jonne Helenius
    •  & Ari Helenius

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https://doi.org/10.1038/356260a0

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