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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...

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Autores principales: Yang, Xiuwei, Kovalenko, Oleg V., Tang, Wei, Claas, Christoph, Stipp, Christopher S., Hemler, Martin E.
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 2004
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.
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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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