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

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Identification of the PDI-family member ERp90 as an interaction partner of ERFAD. / Riemer, Jan; Hansen, Henning G; Appenzeller-Herzog, C. ; Appenzeller-Herzog, Christian; Johansson, Linda; Ellgaard, Lars.

I: P L o S One, Bind 6, Nr. 2, 2011.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

Riemer, J, Hansen, HG, Appenzeller-Herzog, C, Appenzeller-Herzog, C, Johansson, L & Ellgaard, L 2011, 'Identification of the PDI-family member ERp90 as an interaction partner of ERFAD', P L o S One, bind 6, nr. 2. https://doi.org/10.1371/journal.pone.0017037

APA

Riemer, J., Hansen, H. G., Appenzeller-Herzog, C., Appenzeller-Herzog, C., Johansson, L., & Ellgaard, L. (2011). Identification of the PDI-family member ERp90 as an interaction partner of ERFAD. P L o S One, 6(2). https://doi.org/10.1371/journal.pone.0017037

Vancouver

Riemer J, Hansen HG, Appenzeller-Herzog C, Appenzeller-Herzog C, Johansson L, Ellgaard L. Identification of the PDI-family member ERp90 as an interaction partner of ERFAD. P L o S One. 2011;6(2). https://doi.org/10.1371/journal.pone.0017037

Author

Riemer, Jan ; Hansen, Henning G ; Appenzeller-Herzog, C. ; Appenzeller-Herzog, Christian ; Johansson, Linda ; Ellgaard, Lars. / Identification of the PDI-family member ERp90 as an interaction partner of ERFAD. I: P L o S One. 2011 ; Bind 6, Nr. 2.

Bibtex

@article{a20e7a76a09e435f8a05fd5c498c5003,

title = "Identification of the PDI-family member ERp90 as an interaction partner of ERFAD",

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.",

author = "Jan Riemer and Hansen, {Henning G} and C. Appenzeller-Herzog and Christian Appenzeller-Herzog and Linda Johansson and Lars Ellgaard",

note = "Artikel ID: e17037",

year = "2011",

doi = "10.1371/journal.pone.0017037",

language = "English",

volume = "6",

journal = "PLoS ONE",

issn = "1932-6203",

publisher = "Public Library of Science",

number = "2",

}

RIS

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

VL - 6

JO - PLoS ONE

JF - PLoS ONE

SN - 1932-6203

IS - 2

ER -

ID: 33959358