ERO1-like protein alpha

Definition:

Oxidoreductase involved in disulfide bond formation in the endoplasmic reticulum. Efficiently reoxidizes P4HB/PDI, the enzyme catalyzing protein disulfide formation, in order to allow P4HB to sustain additional rounds of disulfide formation. Following P4HB reoxidation, passes its electrons to molecular oxygen via FAD, leading to the production of reactive oxygen species (ROS) in the cell. Required for the proper folding of immunoglobulins. Plays an important role in ER stress-induced, CHOP-dependent apoptosis by activating the inositol 1,4,5-trisphosphate receptor IP3R1. Involved in the release of the unfolded cholera toxin from reduced P4HB/PDI in case of infection by V.cholerae, thereby playing a role in retrotranslocation of the toxin.

References:

[1]. A Mezghrani, et al. Manipulation of oxidative protein folding and PDI redox state in mammalian cells. EMBO J. 2001 Nov 15;20(22):6288-96. [Content Brief]

[2]. A M Benham, et al. The CXXCXXC motif determines the folding, structure and stability of human Ero1-Lalpha. EMBO J. 2000 Sep 1;19(17):4493-502. [Content Brief]

[3]. A Cabibbo, et al. ERO1-L, a human protein that favors disulfide bond formation in the endoplasmic reticulum. J Biol Chem. 2000 Feb 18;275(7):4827-33. [Content Brief]

[4]. Jianchao Zhang, et al. Secretory kinase Fam20C tunes endoplasmic reticulum redox state via phosphorylation of Ero1α. EMBO J. 2018 Jul 13;37(14):e98699. [Content Brief]

[5]. Christian Appenzeller-Herzog, et al. A novel disulphide switch mechanism in Ero1alpha balances ER oxidation in human cells. EMBO J. 2008 Nov 19;27(22):2977-87. [Content Brief]

[6]. Karl M Baker, et al. Low reduction potential of Ero1alpha regulatory disulphides ensures tight control of substrate oxidation. EMBO J. 2008 Nov 19;27(22):2988-97. [Content Brief]

[7]. Henning Gram Hansen, et al. Hyperactivity of the Ero1α oxidase elicits endoplasmic reticulum stress but no broad antioxidant response. J Biol Chem. 2012 Nov 16;287(47):39513-23. [Content Brief]

[8]. Billy Tsai, et al. Unfolded cholera toxin is transferred to the ER membrane and released from protein disulfide isomerase upon oxidation by Ero1. J Cell Biol. 2002 Oct 28;159(2):207-16. [Content Brief]

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