Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1986-2-19
pubmed:abstractText
The human asialoglycoprotein receptor H1 is anchored in the membrane by a single stretch of 20 hydrophobic amino acids; the hydrophilic amino terminus faces the cytoplasm, and the carboxyl terminus is exoplasmic. We show here that glycosylation and insertion of the asialoglycoprotein receptor into the endoplasmic reticulum membrane is cotranslational and SRP-dependent and occurs without proteolytic cleavage. The membrane-anchor domain is necessary for membrane insertion, since a receptor with the segment deleted is neither inserted nor glycosylated. The segment is also sufficient for membrane insertion, since it will initiate translocation of a carboxy-terminal domain of rat alpha-tubulin across the membrane. We propose that a helical hairpin mechanism of membrane insertion is used both by cleaved amino-terminal and uncleaved internal signal sequences.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0092-8674
pubmed:author
pubmed:issnType
Print
pubmed:day
17
pubmed:volume
44
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
177-85
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1986
pubmed:articleTitle
An internal signal sequence: the asialoglycoprotein receptor membrane anchor.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't