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Differential stability of tetraspanin/tetraspanin interactions: role of palmitoylation
Author(s) -
Charrin Stéphanie,
Manié Serge,
Oualid Michael,
Billard Martine,
Boucheix Claude,
Rubinstein Eric
Publication year - 2002
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(02)02522-x
Subject(s) - tetraspanin , cd81 , palmitoylation , microbiology and biotechnology , chemistry , biology , biochemistry , virology , virus , cell , hepatitis c virus , cysteine , enzyme
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 [ 3 H]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.