Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2007-1-10
pubmed:abstractText
ERp57 is a member of the protein disulphide isomerase family of oxidoreductases, which are involved in native disulphide bond formation in the endoplasmic reticulum of mammalian cells. This enzyme has been shown to be associated with both calnexin and calreticulin and, therefore, has been proposed to be a glycoprotein-specific oxidoreductase. Here, we identify endogenous substrates for ERp57 by trapping mixed disulphide intermediates between enzyme and substrate. Our results demonstrate that the substrates for this enzyme are mostly heavily glycosylated, disulphide bonded proteins. In addition, we show that the substrate proteins share common structural domains, indicating that substrate specificity may involve specific structural features as well as the presence of an oligosaccharide side chain. We also show that the folding of two of the endogenous substrates for ERp57 is impaired in ERp57 knockout cells and that prevention of an interaction with calnexin or calreticulin perturbs the folding of some, but not all, substrates with multiple disulphide bonds. These results suggest a specific role for ERp57 in the isomerisation of non-native disulphide bonds in specific glycoprotein substrates.
pubmed:grant
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/17170699-10085220, http://linkedlifedata.com/resource/pubmed/commentcorrection/17170699-10436013, http://linkedlifedata.com/resource/pubmed/commentcorrection/17170699-10573423, http://linkedlifedata.com/resource/pubmed/commentcorrection/17170699-11134056, http://linkedlifedata.com/resource/pubmed/commentcorrection/17170699-11419950, http://linkedlifedata.com/resource/pubmed/commentcorrection/17170699-11697912, http://linkedlifedata.com/resource/pubmed/commentcorrection/17170699-11707400, http://linkedlifedata.com/resource/pubmed/commentcorrection/17170699-11885293, http://linkedlifedata.com/resource/pubmed/commentcorrection/17170699-12032078, http://linkedlifedata.com/resource/pubmed/commentcorrection/17170699-12415301, http://linkedlifedata.com/resource/pubmed/commentcorrection/17170699-12493918, http://linkedlifedata.com/resource/pubmed/commentcorrection/17170699-14189872, http://linkedlifedata.com/resource/pubmed/commentcorrection/17170699-14699087, http://linkedlifedata.com/resource/pubmed/commentcorrection/17170699-14739460, http://linkedlifedata.com/resource/pubmed/commentcorrection/17170699-14871896, http://linkedlifedata.com/resource/pubmed/commentcorrection/17170699-14871899, http://linkedlifedata.com/resource/pubmed/commentcorrection/17170699-1523409, http://linkedlifedata.com/resource/pubmed/commentcorrection/17170699-15507438, http://linkedlifedata.com/resource/pubmed/commentcorrection/17170699-15608170, http://linkedlifedata.com/resource/pubmed/commentcorrection/17170699-15643448, http://linkedlifedata.com/resource/pubmed/commentcorrection/17170699-15652484, http://linkedlifedata.com/resource/pubmed/commentcorrection/17170699-16193070, http://linkedlifedata.com/resource/pubmed/commentcorrection/17170699-16311600, http://linkedlifedata.com/resource/pubmed/commentcorrection/17170699-16368681, http://linkedlifedata.com/resource/pubmed/commentcorrection/17170699-16407314, http://linkedlifedata.com/resource/pubmed/commentcorrection/17170699-16677074, http://linkedlifedata.com/resource/pubmed/commentcorrection/17170699-1988050, http://linkedlifedata.com/resource/pubmed/commentcorrection/17170699-3173483, http://linkedlifedata.com/resource/pubmed/commentcorrection/17170699-7499282, http://linkedlifedata.com/resource/pubmed/commentcorrection/17170699-7723011, http://linkedlifedata.com/resource/pubmed/commentcorrection/17170699-7741697, http://linkedlifedata.com/resource/pubmed/commentcorrection/17170699-7773751, http://linkedlifedata.com/resource/pubmed/commentcorrection/17170699-8385607, http://linkedlifedata.com/resource/pubmed/commentcorrection/17170699-8974399, http://linkedlifedata.com/resource/pubmed/commentcorrection/17170699-9430631, http://linkedlifedata.com/resource/pubmed/commentcorrection/17170699-9497314, http://linkedlifedata.com/resource/pubmed/commentcorrection/17170699-9746345
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0261-4189
pubmed:author
pubmed:issnType
Print
pubmed:day
10
pubmed:volume
26
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
28-40
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed:year
2007
pubmed:articleTitle
ERp57 is essential for efficient folding of glycoproteins sharing common structural domains.
pubmed:affiliation
Faculty of Life Sciences, University of Manchester, Manchester, UK.
pubmed:publicationType
Journal Article
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