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

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  • Jan Riemer
  • Henning G Hansen
  • C. Appenzeller-Herzog
  • Christian Appenzeller-Herzog
  • Linda Johansson
  • Ellgaard, Lars
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.
TidsskriftP L o S One
Udgave nummer2
Antal sider9
StatusUdgivet - 2011

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Artikel ID: e17037

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