Palmitoylation of Tetraspanin Proteins: Modulation of CD151 Lateral Interactions, Subcellular Distribution, and Integrin-dependent Cell Morphology
| العنوان: | Palmitoylation of Tetraspanin Proteins: Modulation of CD151 Lateral Interactions, Subcellular Distribution, and Integrin-dependent Cell Morphology |
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| المؤلفون: | Martin E. Hemler, Lan Bo Chen, Zemin Wang, Xiuwei Yang, Christoph Claas, Jordan A. Kreidberg, Stine-Kathrein Kraeft |
| المصدر: | Molecular Biology of the Cell. 13:767-781 |
| بيانات النشر: | American Society for Cell Biology (ASCB), 2002. |
| سنة النشر: | 2002 |
| مصطلحات موضوعية: | Recombinant Fusion Proteins, Green Fluorescent Proteins, Molecular Sequence Data, Integrin, Palmitates, Nerve Tissue Proteins, Tetraspanin 24, Biology, Cell morphology, Article, Cell Line, symbols.namesake, Palmitoylation, Tetraspanin, Antigens, CD, Humans, Amino Acid Sequence, Molecular Biology, Cell Size, Protein Synthesis Inhibitors, Brefeldin A, Integrin alpha3beta1, Membrane Proteins, Biological Transport, Cell Biology, Golgi apparatus, Cell biology, Luminescent Proteins, Membrane protein, embryonic structures, Mutagenesis, Site-Directed, biology.protein, symbols, Indicators and Reagents, lipids (amino acids, peptides, and proteins), Sequence Alignment, Intracellular |
| الوصف: | Here we demonstrate that multiple tetraspanin (transmembrane 4 superfamily) proteins are palmitoylated, in either the Golgi or a post-Golgi compartment. Using CD151 as a model tetraspanin, we identified and mutated intracellular N-terminal and C-terminal cysteine palmitoylation sites. Simultaneous mutations of C11, C15, C242, and C243 (each to serine) eliminated >90% of CD151 palmitoylation. Notably, palmitoylation had minimal influence on the density of tetraspanin protein complexes, did not promote tetraspanin localization into detergent-resistant microdomains, and was not required for CD151-α3β1 integrin association. However, the CD151 tetra mutant showed markedly diminished associations with other cell surface proteins, including other transmembrane 4 superfamily proteins (CD9, CD63). Thus, palmitoylation may be critical for assembly of the large network of cell surface tetraspanin-protein interactions, sometimes called the “tetraspanin web.” Also, compared with wild-type CD151, the tetra mutant was much more diffusely distributed and showed markedly diminished stability during biosynthesis. Finally, expression of the tetra-CD151 mutant profoundly altered α3 integrin-deficient kidney epithelial cells, such that they converted from a dispersed, elongated morphology to an epithelium-like cobblestone clustering. These results point to novel biochemical and biological functions for tetraspanin palmitoylation. |
| تدمد: | 1939-4586 1059-1524 |
| DOI: | 10.1091/mbc.01-05-0275 |
| URL الوصول: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d1e873a150ff29ed619d642a1797882e https://doi.org/10.1091/mbc.01-05-0275 |
| Rights: | OPEN |
| رقم الانضمام: | edsair.doi.dedup.....d1e873a150ff29ed619d642a1797882e |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 19394586 10591524 |
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| DOI: | 10.1091/mbc.01-05-0275 |