Identification of the PDI-family member ERp90 as an interaction partner of ERFAD

TY - JOUR

T1 - Identification of the PDI-family member ERp90 as an interaction partner of ERFAD

AU - Riemer, Jan

AU - Hansen, Henning G

AU - Appenzeller-Herzog, C.

AU - Appenzeller-Herzog, Christian

AU - Johansson, Linda

AU - Ellgaard, Lars

N1 - Artikel ID: e17037

PY - 2011

Y1 - 2011

N2 - 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.

AB - 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.

U2 - 10.1371/journal.pone.0017037

DO - 10.1371/journal.pone.0017037

M3 - Journal article

C2 - 21359175

SN - 1932-6203

VL - 6

JO - P L o S One

JF - P L o S One

IS - 2

ER -