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Public Library of Science, PLoS ONE, 2(6), p. e17037, 2011

DOI: 10.1371/journal.pone.0017037

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Identification of the PDI-Family Member ERp90 as an Interaction Partner of ERFAD

Journal article published in 2011 by Jan Riemer, Henning G. Hansen, Christian Appenzeller-Herzog ORCID, Linda Johansson, Lars Ellgaard ORCID
This paper is made freely available by the publisher.
This paper is made freely available by the publisher.

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Abstract

In the endoplasmic reticulum (ER), members of the protein disulfide isomerase (PDI) family perform critical functions during protein maturation. Herein, we identify the previously uncharacterized PDI-family member ERp90. In cultured human cells, we find ERp90 to be a soluble ER-luminal glycoprotein that comprises five potential thioredoxin (Trx)-like domains. Mature ERp90 contains 10 cysteine residues, of which at least some form intramolecular disulfides. While none of the Trx domains contain a canonical Cys-Xaa-Xaa-Cys active-site motif, other conserved cysteines could endow the protein with redox activity. Importantly, we show that ERp90 co-immunoprecipitates with ERFAD, a flavoprotein involved in ER-associated degradation (ERAD), through what is most likely a direct interaction. We propose that the function of ERp90 is related to substrate recruitment or delivery to the ERAD retrotranslocation machinery by ERFAD.