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

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...

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Autores principales:	Jan Riemer, Henning G Hansen, Christian Appenzeller-Herzog, Linda Johansson, Lars Ellgaard
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2011
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/4f58686052c34df6b53f808db4c43678
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spelling	oai:doaj.org-article:4f58686052c34df6b53f808db4c436782021-11-18T06:58:44ZIdentification of the PDI-family member ERp90 as an interaction partner of ERFAD.1932-620310.1371/journal.pone.0017037https://doaj.org/article/4f58686052c34df6b53f808db4c436782011-02-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/21359175/pdf/?tool=EBIhttps://doaj.org/toc/1932-6203In 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.Jan RiemerHenning G HansenChristian Appenzeller-HerzogLinda JohanssonLars EllgaardPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 6, Iss 2, p e17037 (2011)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Jan Riemer Henning G Hansen Christian Appenzeller-Herzog Linda Johansson Lars Ellgaard Identification of the PDI-family member ERp90 as an interaction partner of ERFAD.
description	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.
format	article
author	Jan Riemer Henning G Hansen Christian Appenzeller-Herzog Linda Johansson Lars Ellgaard
author_facet	Jan Riemer Henning G Hansen Christian Appenzeller-Herzog Linda Johansson Lars Ellgaard
author_sort	Jan Riemer
title	Identification of the PDI-family member ERp90 as an interaction partner of ERFAD.
title_short	Identification of the PDI-family member ERp90 as an interaction partner of ERFAD.
title_full	Identification of the PDI-family member ERp90 as an interaction partner of ERFAD.
title_fullStr	Identification of the PDI-family member ERp90 as an interaction partner of ERFAD.
title_full_unstemmed	Identification of the PDI-family member ERp90 as an interaction partner of ERFAD.
title_sort	identification of the pdi-family member erp90 as an interaction partner of erfad.
publisher	Public Library of Science (PLoS)
publishDate	2011
url	https://doaj.org/article/4f58686052c34df6b53f808db4c43678
work_keys_str_mv	AT janriemer identificationofthepdifamilymembererp90asaninteractionpartneroferfad AT henningghansen identificationofthepdifamilymembererp90asaninteractionpartneroferfad AT christianappenzellerherzog identificationofthepdifamilymembererp90asaninteractionpartneroferfad AT lindajohansson identificationofthepdifamilymembererp90asaninteractionpartneroferfad AT larsellgaard identificationofthepdifamilymembererp90asaninteractionpartneroferfad
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Identification of the PDI-family member ERp90 as an interaction partner of ERFAD.

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