Linked Life Data

7574493

Source:http://linkedlifedata.com/resource/pubmed/id/7574493

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
1995-11-3
pubmed:abstractText
Glycosylphosphatidylinositol (GPI) linkage is a fairly common means of anchoring membrane proteins to eukaryotic cells, although the exact function of the GPI linkage is not clear. The nascent form of a typical GPI protein contains a hydrophobic NH2-terminal signal peptide that directs it to the ER. There the signal peptide is removed by NH2-terminal signal peptidase. Nascent forms of GPI-linked proteins contain a second hydrophobic peptide at their COOH terminus. The COOH-terminal peptide is also removed during processing and the GPI moiety is ultimately linked to what had been an internal sequence in the nascent protein. Two independent pathways are involved in the biosynthesis of GPI proteins, GPI formation, and processing of the nascent protein with attachment of the GPI moiety. Studies in whole cells and in cell-free systems indicate that structural requirements around the COOH-terminal cleavage site of nascent proteins are similar to those at the cleavage site of NH2-terminal signal peptidase. However, COOH-terminal processing requires a transmidase for which evidence is presented as well as a proposed mechanism of its action.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0066-4154
pubmed:author
pubmed:issnType
Print
pubmed:volume
64
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
563-91
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1995
pubmed:articleTitle
How glycosylphosphatidylinositol-anchored membrane proteins are made.
pubmed:affiliation
Roche Institute of Molecular Biology, Roche Research Center, Nutley, New Jersey 07110, USA.
pubmed:publicationType
Journal Article, Review