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

Publikation: Bidrag til tidsskriftTidsskriftartikelfagfællebedømt

Dokumenter

  • 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.
OriginalsprogEngelsk
TidsskriftP L o S One
Vol/bind6
Udgave nummer2
Antal sider9
ISSN1932-6203
DOI
StatusUdgivet - 2011

Bibliografisk note

Artikel ID: e17037

Antal downloads er baseret på statistik fra Google Scholar og www.ku.dk


Ingen data tilgængelig

ID: 33959358