Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1-3
pubmed:dateCreated
2002-4-17
pubmed:abstractText
The tetraspanins associate with various surface molecules and with each other to build a network of molecular interactions, the tetraspanin web. The interaction of tetraspanins with each other seems to be central for the assembly of the tetraspanin web. All tetraspanins studied, CD9, CD37, CD53, CD63, CD81, CD82 and CD151, were found to incorporate [3H]palmitate. By site-directed mutagenesis, CD9 was found to be palmitoylated at any of the four internal juxtamembrane regions. The palmitoylation of CD9 did not influence the partition in detergent-resistant membranes but contributed to the interaction with CD81 and CD53. In particular, the resistance of the CD9/CD81 interaction to EDTA, which disrupts other tetraspanin/tetraspanin interactions, was entirely dependent on palmitoylation.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD, http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD53, http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD81, http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD9, http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Differentiation..., http://linkedlifedata.com/resource/pubmed/chemical/CD53 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/CD81 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/CD9 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Cysteine, http://linkedlifedata.com/resource/pubmed/chemical/Detergents, http://linkedlifedata.com/resource/pubmed/chemical/Macromolecular Substances, http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins, http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Palmitic Acid, http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0014-5793
pubmed:author
pubmed:issnType
Print
pubmed:day
10
pubmed:volume
516
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
139-44
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed-meshheading:11959120-Animals, pubmed-meshheading:11959120-Antigens, CD, pubmed-meshheading:11959120-Antigens, CD53, pubmed-meshheading:11959120-Antigens, CD81, pubmed-meshheading:11959120-Antigens, CD9, pubmed-meshheading:11959120-Antigens, Differentiation, T-Lymphocyte, pubmed-meshheading:11959120-CHO Cells, pubmed-meshheading:11959120-Cell Line, pubmed-meshheading:11959120-Cricetinae, pubmed-meshheading:11959120-Cysteine, pubmed-meshheading:11959120-Detergents, pubmed-meshheading:11959120-Drug Stability, pubmed-meshheading:11959120-Humans, pubmed-meshheading:11959120-Macromolecular Substances, pubmed-meshheading:11959120-Membrane Glycoproteins, pubmed-meshheading:11959120-Membrane Proteins, pubmed-meshheading:11959120-Mutagenesis, Site-Directed, pubmed-meshheading:11959120-Palmitic Acid, pubmed-meshheading:11959120-Recombinant Proteins
pubmed:year
2002
pubmed:articleTitle
Differential stability of tetraspanin/tetraspanin interactions: role of palmitoylation.
pubmed:affiliation
INSERM U268, Hôpital Paul Brousse, 94807 Cedex, Villejuif, France.
pubmed:publicationType
Journal Article, In Vitro, Research Support, Non-U.S. Gov't