Skip to main content

Research Repository

Advanced Search

The CXXCXXC motif determines the folding, structure and stability of human Ero1-La.

Benham, A.M.; Cabibbo, A.; Fassio, A.; Bulleid, N.; Sitia, R.; Braakman, I.

Authors

A. Cabibbo

A. Fassio

N. Bulleid

R. Sitia

I. Braakman



Abstract

The presence of correctly formed disulfide bonds is crucial to the structure and function of proteins that are synthesized in the endoplasmic reticulum (ER). Disulfide bond formation occurs in the ER owing to the presence of several specialized catalysts and a suitable redox potential. Work in yeast has indicated that the ER resident glycoprotein Ero1p provides oxidizing equivalents to newly synthesized proteins via protein disulfide isomerase (PDI). Here we show that Ero1‐Lα, the human homolog of Ero1p, exists as a collection of oxidized and reduced forms and covalently binds PDI. We analyzed Ero1‐Lα cysteine mutants in the presumed active site C391VGCFKC397. Our results demonstrate that this motif is important for protein folding, structural integrity, protein half‐life and the stability of the Ero1‐Lα–PDI complex.

Citation

Benham, A., Cabibbo, A., Fassio, A., Bulleid, N., Sitia, R., & Braakman, I. (2000). The CXXCXXC motif determines the folding, structure and stability of human Ero1-La. The EMBO Journal, 19(17), 4493-4502. https://doi.org/10.1093/emboj/19.17.4493

Journal Article Type Article
Acceptance Date Jul 12, 2000
Online Publication Date Sep 1, 2000
Publication Date 2000-09
Journal EMBO Journal
Print ISSN 0261-4189
Electronic ISSN 1460-2075
Publisher EMBO Press
Peer Reviewed Peer Reviewed
Volume 19
Issue 17
Pages 4493-4502
DOI https://doi.org/10.1093/emboj/19.17.4493