Linked Life Data

9654106

Source:http://linkedlifedata.com/resource/pubmed/id/9654106

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1998-7-17
pubmed:abstractText
Plasma membrane receptors are retrieved continually from the cell surface by endocytosis and transported to intracellular organelles. They are internalized at various rates depending on their ability to interact with endocytic structures of the plasma membrane. The interleukin-2-receptor beta chain is endocytosed constitutively and efficiently. Here we show that different motifs in its cytosolic tail promote entry in an additive way, each of them acting as a weak internalization signal. The transmembrane domain of beta also participates in endocytosis. In conclusion, several weak endocytic determinants can be responsible for the rapid internalization of a membrane protein.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0014-2956
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
253
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
525-30
pubmed:dateRevised
2007-7-23
pubmed:meshHeading
pubmed:year
1998
pubmed:articleTitle
Several weak signals in the cytosolic and transmembrane domains of the interleukin-2-receptor beta chain allow for its efficient endocytosis.
pubmed:affiliation
Unité de Biologie des Interactions Cellulaires, URA CNRS 1960, Institut Pasteur, Paris, France.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't