Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
10
pubmed:dateCreated
1993-5-5
pubmed:abstractText
The erd2 protein is the receptor responsible for recycling proteins bearing the carboxyl-terminal sequence KDEL (single-letter amino acid code) to the endoplasmic reticulum, following their loss from that organelle by the process of forward transport. To study the interaction of erd2p with the sequence KDEL we have reconstituted binding of erd2p to its ligand in vitro. Binding in vitro exhibits the same sequence specificity as retention of lumenal proteins in vivo and is strikingly sensitive to pH. Our results raise the possibility that erd2p-mediated sorting of lumenal endoplasmic reticulum proteins is facilitated by the pH differences between compartments of the secretory pathway.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
5
pubmed:volume
268
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
7465-8
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
pH-dependent binding of KDEL to its receptor in vitro.
pubmed:affiliation
Medical Research Council Laboratory of Molecular Biology, Cambridge, United Kingdom.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't