The Sec63p J-domain is required for ERAD of soluble proteins in yeast.

How misfolded proteins are exported from the ER to the cytosol for degradation (ER-associated Degradation, ERAD) and which proteins are participating in this process is not understood. Several studies using a single, leaky mutant indicated that Sec63p might be involved in ERAD. More recently, Sec63p...

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Autores principales:	Christina Servas, Karin Römisch
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2013
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/e5241ed9947846919e346a6d1ddb9377
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spelling	oai:doaj.org-article:e5241ed9947846919e346a6d1ddb93772021-11-18T08:43:29ZThe Sec63p J-domain is required for ERAD of soluble proteins in yeast.1932-620310.1371/journal.pone.0082058https://doaj.org/article/e5241ed9947846919e346a6d1ddb93772013-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/24324744/?tool=EBIhttps://doaj.org/toc/1932-6203How misfolded proteins are exported from the ER to the cytosol for degradation (ER-associated Degradation, ERAD) and which proteins are participating in this process is not understood. Several studies using a single, leaky mutant indicated that Sec63p might be involved in ERAD. More recently, Sec63p was also found strongly associated with proteasomes attached to the protein-conducting channel in the ER membrane which presumably form part of the export machinery. These observations prompted us to reinvestigate the role of Sec63p in ERAD by generating new mutants which were selected in a screen monitoring the intracellular accumulation of the ERAD substrate CPY*. We show that a mutation in the DnaJ-domain of Sec63p causes a defect in ERAD, whereas mutations in the Brl, acidic, and transmembrane domains only affect protein import into the ER. Unexpectedly, mutations in the acidic domain which mediates interaction of Sec63p with Sec62p also caused defects in cotranslational import. In contrast to mammalian cells where SEC63 expression levels affect steady-state levels of multi-spanning transmembrane proteins, the sec63 J-domain mutant was only defective in ERAD of soluble substrates.Christina ServasKarin RömischPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 8, Iss 12, p e82058 (2013)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Christina Servas Karin Römisch The Sec63p J-domain is required for ERAD of soluble proteins in yeast.
description	How misfolded proteins are exported from the ER to the cytosol for degradation (ER-associated Degradation, ERAD) and which proteins are participating in this process is not understood. Several studies using a single, leaky mutant indicated that Sec63p might be involved in ERAD. More recently, Sec63p was also found strongly associated with proteasomes attached to the protein-conducting channel in the ER membrane which presumably form part of the export machinery. These observations prompted us to reinvestigate the role of Sec63p in ERAD by generating new mutants which were selected in a screen monitoring the intracellular accumulation of the ERAD substrate CPY*. We show that a mutation in the DnaJ-domain of Sec63p causes a defect in ERAD, whereas mutations in the Brl, acidic, and transmembrane domains only affect protein import into the ER. Unexpectedly, mutations in the acidic domain which mediates interaction of Sec63p with Sec62p also caused defects in cotranslational import. In contrast to mammalian cells where SEC63 expression levels affect steady-state levels of multi-spanning transmembrane proteins, the sec63 J-domain mutant was only defective in ERAD of soluble substrates.
format	article
author	Christina Servas Karin Römisch
author_facet	Christina Servas Karin Römisch
author_sort	Christina Servas
title	The Sec63p J-domain is required for ERAD of soluble proteins in yeast.
title_short	The Sec63p J-domain is required for ERAD of soluble proteins in yeast.
title_full	The Sec63p J-domain is required for ERAD of soluble proteins in yeast.
title_fullStr	The Sec63p J-domain is required for ERAD of soluble proteins in yeast.
title_full_unstemmed	The Sec63p J-domain is required for ERAD of soluble proteins in yeast.
title_sort	sec63p j-domain is required for erad of soluble proteins in yeast.
publisher	Public Library of Science (PLoS)
publishDate	2013
url	https://doaj.org/article/e5241ed9947846919e346a6d1ddb9377
work_keys_str_mv	AT christinaservas thesec63pjdomainisrequiredforeradofsolubleproteinsinyeast AT karinromisch thesec63pjdomainisrequiredforeradofsolubleproteinsinyeast AT christinaservas sec63pjdomainisrequiredforeradofsolubleproteinsinyeast AT karinromisch sec63pjdomainisrequiredforeradofsolubleproteinsinyeast
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The Sec63p J-domain is required for ERAD of soluble proteins in yeast.

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