Abstract
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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Animals
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Antigens, CD / chemistry*
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Antigens, CD / genetics
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Antigens, CD / metabolism*
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Antigens, Differentiation, T-Lymphocyte / chemistry
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Antigens, Differentiation, T-Lymphocyte / genetics
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Antigens, Differentiation, T-Lymphocyte / metabolism
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CHO Cells
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Cell Line
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Cricetinae
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Cysteine / chemistry
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Cysteine / genetics
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Detergents
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Drug Stability
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Humans
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In Vitro Techniques
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Macromolecular Substances
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Membrane Glycoproteins*
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Membrane Proteins / chemistry
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Membrane Proteins / genetics
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Membrane Proteins / metabolism*
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Mutagenesis, Site-Directed
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Palmitic Acid / chemistry
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Recombinant Proteins / chemistry
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Recombinant Proteins / genetics
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Recombinant Proteins / metabolism
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Tetraspanin 25
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Tetraspanin 28
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Tetraspanin 29
Substances
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Antigens, CD
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Antigens, Differentiation, T-Lymphocyte
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CD53 protein, human
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CD81 protein, human
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CD9 protein, human
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Detergents
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Macromolecular Substances
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Membrane Glycoproteins
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Membrane Proteins
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Recombinant Proteins
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Tetraspanin 25
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Tetraspanin 28
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Tetraspanin 29
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Palmitic Acid
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Cysteine