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Palmitoylation supports assembly and function of integrin–tetraspanin complexes
As observed previously, tetraspanin palmitoylation promotes tetraspanin microdomain assembly. Here, we show that palmitoylated integrins (α3, α6, and β4 subunits) and tetraspanins (CD9, CD81, and CD63) coexist in substantially overlapping complexes. Removal of β4 palmitoylation sites markedly impair...
Autores principales: | , , , , , |
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Formato: | Texto |
Lenguaje: | English |
Publicado: |
The Rockefeller University Press
2004
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2172609/ https://www.ncbi.nlm.nih.gov/pubmed/15611341 http://dx.doi.org/10.1083/jcb.200404100 |
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author | Yang, Xiuwei Kovalenko, Oleg V. Tang, Wei Claas, Christoph Stipp, Christopher S. Hemler, Martin E. |
author_facet | Yang, Xiuwei Kovalenko, Oleg V. Tang, Wei Claas, Christoph Stipp, Christopher S. Hemler, Martin E. |
author_sort | Yang, Xiuwei |
collection | PubMed |
description | As observed previously, tetraspanin palmitoylation promotes tetraspanin microdomain assembly. Here, we show that palmitoylated integrins (α3, α6, and β4 subunits) and tetraspanins (CD9, CD81, and CD63) coexist in substantially overlapping complexes. Removal of β4 palmitoylation sites markedly impaired cell spreading and signaling through p130Cas on laminin substrate. Also in palmitoylation-deficient β4, secondary associations with tetraspanins (CD9, CD81, and CD63) were diminished and cell surface CD9 clustering was decreased, whereas core α6β4–CD151 complex formation was unaltered. There is also a functional connection between CD9 and β4 integrins, as evidenced by anti-CD9 antibody effects on β4-dependent cell spreading. Notably, β4 palmitoylation neither increased localization into “light membrane” fractions of sucrose gradients nor decreased solubility in nonionic detergents—hence it does not promote lipid raft association. Instead, palmitoylation of β4 (and of the closely associated tetraspanin CD151) promotes CD151–α6β4 incorporation into a network of secondary tetraspanin interactions (with CD9, CD81, CD63, etc.), which provides a novel framework for functional regulation. |
format | Text |
id | pubmed-2172609 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2004 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-21726092008-03-05 Palmitoylation supports assembly and function of integrin–tetraspanin complexes Yang, Xiuwei Kovalenko, Oleg V. Tang, Wei Claas, Christoph Stipp, Christopher S. Hemler, Martin E. J Cell Biol Research Articles As observed previously, tetraspanin palmitoylation promotes tetraspanin microdomain assembly. Here, we show that palmitoylated integrins (α3, α6, and β4 subunits) and tetraspanins (CD9, CD81, and CD63) coexist in substantially overlapping complexes. Removal of β4 palmitoylation sites markedly impaired cell spreading and signaling through p130Cas on laminin substrate. Also in palmitoylation-deficient β4, secondary associations with tetraspanins (CD9, CD81, and CD63) were diminished and cell surface CD9 clustering was decreased, whereas core α6β4–CD151 complex formation was unaltered. There is also a functional connection between CD9 and β4 integrins, as evidenced by anti-CD9 antibody effects on β4-dependent cell spreading. Notably, β4 palmitoylation neither increased localization into “light membrane” fractions of sucrose gradients nor decreased solubility in nonionic detergents—hence it does not promote lipid raft association. Instead, palmitoylation of β4 (and of the closely associated tetraspanin CD151) promotes CD151–α6β4 incorporation into a network of secondary tetraspanin interactions (with CD9, CD81, CD63, etc.), which provides a novel framework for functional regulation. The Rockefeller University Press 2004-12-20 /pmc/articles/PMC2172609/ /pubmed/15611341 http://dx.doi.org/10.1083/jcb.200404100 Text en Copyright © 2004, The Rockefeller University Press This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/). |
spellingShingle | Research Articles Yang, Xiuwei Kovalenko, Oleg V. Tang, Wei Claas, Christoph Stipp, Christopher S. Hemler, Martin E. Palmitoylation supports assembly and function of integrin–tetraspanin complexes |
title | Palmitoylation supports assembly and function of integrin–tetraspanin complexes |
title_full | Palmitoylation supports assembly and function of integrin–tetraspanin complexes |
title_fullStr | Palmitoylation supports assembly and function of integrin–tetraspanin complexes |
title_full_unstemmed | Palmitoylation supports assembly and function of integrin–tetraspanin complexes |
title_short | Palmitoylation supports assembly and function of integrin–tetraspanin complexes |
title_sort | palmitoylation supports assembly and function of integrin–tetraspanin complexes |
topic | Research Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2172609/ https://www.ncbi.nlm.nih.gov/pubmed/15611341 http://dx.doi.org/10.1083/jcb.200404100 |
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