Source:http://linkedlifedata.com/resource/pubmed/id/20029959
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
2009-12-28
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pubmed:abstractText |
Retention of misfolded proteins by the endoplasmic reticulum (ER) is a quality control mechanism involving the participation of endogenous chaperones such as calnexin (CANX). CANX interacts with and restricts plasma membrane expression (PME) of the gonadotropin releasing hormone receptor (GnRHR), a G protein-coupled receptor. CANX also interacts with ERP-57 a thiol oxidoreductase chaperone present in the ER. CANX along with ERP-57 promotes the formation of disulfide bond bridges in nascent proteins. The human GnRH receptor (hGnRHR) is stabilized by two disulfide bond bridges (C(14)-C(200) and C(114)-C(196)), that, when broken, lead to a decrease in receptor expression at the plasma membrane. To determine if the presence of chaperones CANX and ERP-57 exerts an influence over membrane routing and second messenger activation, we assessed the effect of various mutants including those with broken disulfide bridges (Cys --> Ala) along with the hGnRHR. The effect of chaperones on mutants was insignificant, whereas the over expression of ERP-57 led to an hGnRHR retention. This effect was further enhanced by cotransfection with cDNA for CANX showing receptor retention by ERP-57 augmented by CANX, suggesting utilization of these chaperones for quality control of the GnRHR.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Calnexin,
http://linkedlifedata.com/resource/pubmed/chemical/Molecular Chaperones,
http://linkedlifedata.com/resource/pubmed/chemical/PDIA3 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Disulfide-Isomerases,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, LHRH
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
1099-0844
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pubmed:author | |
pubmed:copyrightInfo |
2009 John Wiley & Sons, Ltd.
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pubmed:issnType |
Electronic
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pubmed:volume |
28
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
66-73
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pubmed:meshHeading |
pubmed-meshheading:20029959-Amino Acid Substitution,
pubmed-meshheading:20029959-Animals,
pubmed-meshheading:20029959-COS Cells,
pubmed-meshheading:20029959-Calnexin,
pubmed-meshheading:20029959-Cell Membrane,
pubmed-meshheading:20029959-Cercopithecus aethiops,
pubmed-meshheading:20029959-Endoplasmic Reticulum,
pubmed-meshheading:20029959-Humans,
pubmed-meshheading:20029959-Molecular Chaperones,
pubmed-meshheading:20029959-Mutagenesis, Site-Directed,
pubmed-meshheading:20029959-Protein Disulfide-Isomerases,
pubmed-meshheading:20029959-Protein Folding,
pubmed-meshheading:20029959-Receptors, LHRH
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pubmed:year |
2010
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pubmed:articleTitle |
Protein disulfide isomerase chaperone ERP-57 decreases plasma membrane expression of the human GnRH receptor.
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pubmed:affiliation |
Oregon National Primate Research Center, Beaverton, 97006, USA.
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pubmed:publicationType |
Journal Article,
Research Support, N.I.H., Extramural
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