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Lattices, rafts, and scaffolds: domain regulation of receptor signaling at the plasma membrane

The plasma membrane is organized into various subdomains of clustered macromolecules. Such domains include adhesive structures (cellular synapses, substrate adhesions, and cell–cell junctions) and membrane invaginations (clathrin-coated pits and caveolae), as well as less well-defined domains such a...

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Detalles Bibliográficos
Autores principales: Lajoie, Patrick, Goetz, Jacky G., Dennis, James W., Nabi, Ivan R.
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 2009
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2700393/
https://www.ncbi.nlm.nih.gov/pubmed/19398762
http://dx.doi.org/10.1083/jcb.200811059
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author Lajoie, Patrick
Goetz, Jacky G.
Dennis, James W.
Nabi, Ivan R.
author_facet Lajoie, Patrick
Goetz, Jacky G.
Dennis, James W.
Nabi, Ivan R.
author_sort Lajoie, Patrick
collection PubMed
description The plasma membrane is organized into various subdomains of clustered macromolecules. Such domains include adhesive structures (cellular synapses, substrate adhesions, and cell–cell junctions) and membrane invaginations (clathrin-coated pits and caveolae), as well as less well-defined domains such as lipid rafts and lectin-glycoprotein lattices. Domains are organized by specialized scaffold proteins including the intramembranous caveolins, which stabilize lipid raft domains, and the galectins, a family of animal lectins that cross-link glycoproteins forming molecular lattices. We review evidence that these heterogeneous microdomains interact to regulate substratum adhesion and cytokine receptor dynamics at the cell surface.
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spelling pubmed-27003932009-11-04 Lattices, rafts, and scaffolds: domain regulation of receptor signaling at the plasma membrane Lajoie, Patrick Goetz, Jacky G. Dennis, James W. Nabi, Ivan R. J Cell Biol Reviews The plasma membrane is organized into various subdomains of clustered macromolecules. Such domains include adhesive structures (cellular synapses, substrate adhesions, and cell–cell junctions) and membrane invaginations (clathrin-coated pits and caveolae), as well as less well-defined domains such as lipid rafts and lectin-glycoprotein lattices. Domains are organized by specialized scaffold proteins including the intramembranous caveolins, which stabilize lipid raft domains, and the galectins, a family of animal lectins that cross-link glycoproteins forming molecular lattices. We review evidence that these heterogeneous microdomains interact to regulate substratum adhesion and cytokine receptor dynamics at the cell surface. The Rockefeller University Press 2009-05-04 /pmc/articles/PMC2700393/ /pubmed/19398762 http://dx.doi.org/10.1083/jcb.200811059 Text en © 2009 Lajoie et al. 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.jcb.org/misc/terms.shtml). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 3.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/3.0/).
spellingShingle Reviews
Lajoie, Patrick
Goetz, Jacky G.
Dennis, James W.
Nabi, Ivan R.
Lattices, rafts, and scaffolds: domain regulation of receptor signaling at the plasma membrane
title Lattices, rafts, and scaffolds: domain regulation of receptor signaling at the plasma membrane
title_full Lattices, rafts, and scaffolds: domain regulation of receptor signaling at the plasma membrane
title_fullStr Lattices, rafts, and scaffolds: domain regulation of receptor signaling at the plasma membrane
title_full_unstemmed Lattices, rafts, and scaffolds: domain regulation of receptor signaling at the plasma membrane
title_short Lattices, rafts, and scaffolds: domain regulation of receptor signaling at the plasma membrane
title_sort lattices, rafts, and scaffolds: domain regulation of receptor signaling at the plasma membrane
topic Reviews
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2700393/
https://www.ncbi.nlm.nih.gov/pubmed/19398762
http://dx.doi.org/10.1083/jcb.200811059
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