학술/공연/행사

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The endoplasmic reticulum (ER) provides an environment optimized for oxidative protein folding through the action of Ero1p, which generates disulfide bonds and Pdi1p, which receives disulfide bonds from Ero1p and transfers them to substrate proteins. Feedback regulation of Ero1p through reduction and oxidation of regulatory disulfide bonds within Ero1p is essential for maintaining the proper redox balance in the ER and in this paper we show that Pdi1p is a key element of this feedback loop. Accumulated reduced Pdi1p results in the activation of Ero1p by direct reduction of Ero1p regulatory bonds. Conversely, upon depletion of substrates and accumulation of oxidized Pdi1p, Ero1p is inactivated by both autonomous oxidation and Pdi1p-mediated oxidation of Ero1p regulatory bonds. Tight control of Ero1p activity based on the redox state of Pdi1p explains how cells generate the minimum number of disulfide bonds needed for efficient oxidative protein folding.

 

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