Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
17
pubmed:dateCreated
1995-10-27
pubmed:abstractText
The UDP-Glc:glycoprotein glucosyltransferase is a soluble enzyme of the endoplasmic reticulum that glucosylates protein-linked Man7-9GlcNAc2 to form the monoglucosylated derivatives. In vivo the reaction products are immediately deglucosylated by glucosidase II. The glucosyltransferase has a unique property: it glucosylates misfolded, but not native, glycoproteins. It has been proposed that the glucosyltransferase participates, together with calnexin, in the control mechanism by which only properly folded glycoproteins can exit from the endoplasmic reticulum. In this paper it is demonstrated that the glucosyltransferase recognizes two elements in the acceptor substrates: the innermost N-acetylglucosamine unit of the oligosaccharide and protein domains exposed in denatured, but not in native, conformations. Both determinants have to be covalently linked. In many cases the first element is not accessible to macromolecular probes in native conformations. Concerning the protein domains, it is demonstrated here that the glucosyltransferase interacts with hydrophobic amino acids exposed in denatured conformations. More disordered conformations, i.e. those exposing more hydrophobic amino acids, were found to be those having higher glucose acceptor capacity. It is suggested that both accessibility of the innermost N-acetylglucosamine unit and binding to hydrophobic patches determine the exclusive glucosylation of misfolded conformations by the glucosyltransferase.
pubmed:grant
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/7556060-1531024, http://linkedlifedata.com/resource/pubmed/commentcorrection/7556060-1533626, http://linkedlifedata.com/resource/pubmed/commentcorrection/7556060-1731350, http://linkedlifedata.com/resource/pubmed/commentcorrection/7556060-1826090, http://linkedlifedata.com/resource/pubmed/commentcorrection/7556060-1834945, http://linkedlifedata.com/resource/pubmed/commentcorrection/7556060-1840423, http://linkedlifedata.com/resource/pubmed/commentcorrection/7556060-2449095, http://linkedlifedata.com/resource/pubmed/commentcorrection/7556060-2532539, http://linkedlifedata.com/resource/pubmed/commentcorrection/7556060-2540825, http://linkedlifedata.com/resource/pubmed/commentcorrection/7556060-2806566, http://linkedlifedata.com/resource/pubmed/commentcorrection/7556060-3896128, http://linkedlifedata.com/resource/pubmed/commentcorrection/7556060-4290246, http://linkedlifedata.com/resource/pubmed/commentcorrection/7556060-6373756, http://linkedlifedata.com/resource/pubmed/commentcorrection/7556060-6433977, http://linkedlifedata.com/resource/pubmed/commentcorrection/7556060-6437277, http://linkedlifedata.com/resource/pubmed/commentcorrection/7556060-6863289, http://linkedlifedata.com/resource/pubmed/commentcorrection/7556060-6873448, http://linkedlifedata.com/resource/pubmed/commentcorrection/7556060-7902213, http://linkedlifedata.com/resource/pubmed/commentcorrection/7556060-7947771, http://linkedlifedata.com/resource/pubmed/commentcorrection/7556060-7982990, http://linkedlifedata.com/resource/pubmed/commentcorrection/7556060-8049518, http://linkedlifedata.com/resource/pubmed/commentcorrection/7556060-8302866, http://linkedlifedata.com/resource/pubmed/commentcorrection/7556060-8468315
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0261-4189
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
14
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
4196-203
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed:year
1995
pubmed:articleTitle
The molecular basis for the recognition of misfolded glycoproteins by the UDP-Glc:glycoprotein glucosyltransferase.
pubmed:affiliation
Instituto de Investigaciones Bioquímicas Fundación Campomar, Buenos Aires, Argentina.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't