Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
45
pubmed:dateCreated
1998-12-10
pubmed:abstractText
During receptor-mediated endocytosis, most growth factor receptors are transported to late endocytic compartments and degraded. This process is important to control their expression on the cell surface and requires sorting in early endocytic compartments. Little is known about the mechanisms and the signals involved. We have studied the signal involved in targeting the interleukin 2 receptor beta chain (IL2Rbeta), a member of the cytokine receptor superfamily, toward degradation after internalization. We show that a motif of 8 amino acids in the cytosolic tail of IL2Rbeta is sufficient to target a normally recycling receptor toward degradation. Deletion of this signal strongly impairs IL2Rbeta degradation. Further molecular characterization of the motif shows that it does not resemble the well documented tyrosine and dileucine families of trafficking signals.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
6
pubmed:volume
273
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
29424-9
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1998
pubmed:articleTitle
Molecular characterization of the signal responsible for the targeting of the interleukin 2 receptor beta chain toward intracellular degradation.
pubmed:affiliation
Unité de Biologie des Interactions Cellulaires, URA CNRS 1960, Institut Pasteur, 25 rue du Docteur Roux, 75724 Paris Cedex 15, France.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't