Differential stability of tetraspanin/tetraspanin interactions: role of palmitoylation

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, CD6...

Full description

Saved in:
Bibliographic Details
Published in:FEBS letters 2002-04, Vol.516 (1), p.139-144
Main Authors: Charrin, Stéphanie, Manié, Serge, Oualid, Michael, Billard, Martine, Boucheix, Claude, Rubinstein, Eric
Format: Article
Language:English
Subjects:
Animals
Antigens, CD - chemistry
Antigens, CD - genetics
Antigens, CD - metabolism
Antigens, Differentiation, T-Lymphocyte - chemistry
Antigens, Differentiation, T-Lymphocyte - genetics
Antigens, Differentiation, T-Lymphocyte - metabolism
Cell Line
CHO Cells
Cricetinae
Cysteine - chemistry
Cysteine - genetics
Detergent-resistant membrane
Detergents
DRM, detergent-resistant membrane
Drug Stability
Humans
In Vitro Techniques
Interaction
Macromolecular Substances
Membrane Glycoproteins
Membrane Proteins - chemistry
Membrane Proteins - genetics
Membrane Proteins - metabolism
Mutagenesis, Site-Directed
Palmitic Acid - chemistry
Palmitoylation
Recombinant Proteins - chemistry
Recombinant Proteins - genetics
Recombinant Proteins - metabolism
Tetraspanin
Tetraspanin 25
Tetraspanin 28
Tetraspanin 29
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary: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.
ISSN:0014-5793
1873-3468
DOI:10.1016/S0014-5793(02)02522-X