Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6379
pubmed:dateCreated
1992-7-21
pubmed:abstractText
Isolated polypeptide chains of the T-cell antigen receptor complex are degraded or retained in the endoplasmic reticulum (ER). Assembly of the multisubunit complex allows the individual chains to escape retention in the ER and to be expressed on the cell surface. We engineered a series of deletions in the CD3 epsilon subunit of the human T-cell receptor in order to find the sequences responsible for its retention in the ER. Deletion of amino acids 171 to 180 in the cytosolic tail resulted in the cell-surface expression of the isolated chain. This sequence also promotes retention when it is appended to CD4, a plasma membrane protein. Mutagenesis of the 10-amino-acid CD3 epsilon sequence established that the tyrosine and serine residues are important for ER retention. This and other ER retention signals must be hidden when a complete T-cell receptor complex is assembled in order to allow its expression on the cell surface.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0028-0836
pubmed:author
pubmed:issnType
Print
pubmed:day
18
pubmed:volume
357
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
593-6
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:1535117-Amino Acid Sequence, pubmed-meshheading:1535117-Animals, pubmed-meshheading:1535117-Antigens, CD3, pubmed-meshheading:1535117-Antigens, Differentiation, T-Lymphocyte, pubmed-meshheading:1535117-Base Sequence, pubmed-meshheading:1535117-Cell Membrane, pubmed-meshheading:1535117-Endoplasmic Reticulum, pubmed-meshheading:1535117-Gene Expression, pubmed-meshheading:1535117-Golgi Apparatus, pubmed-meshheading:1535117-Humans, pubmed-meshheading:1535117-Mice, pubmed-meshheading:1535117-Molecular Sequence Data, pubmed-meshheading:1535117-Mutagenesis, pubmed-meshheading:1535117-Polymerase Chain Reaction, pubmed-meshheading:1535117-Receptors, Antigen, T-Cell, pubmed-meshheading:1535117-Signal Transduction, pubmed-meshheading:1535117-Structure-Activity Relationship, pubmed-meshheading:1535117-Transfection
pubmed:year
1992
pubmed:articleTitle
An endoplasmic reticulum retention signal in the CD3 epsilon chain of the T-cell receptor.
pubmed:affiliation
Centro de Biología Molecular, Universidad Autónoma de Madrid, CSIC, Spain.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't