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Monomer–dimer dynamics and distribution of GPI-anchored uPAR are determined by cell surface protein assemblies

To search for functional links between glycosylphosphatidylinositol (GPI) protein monomer–oligomer exchange and membrane dynamics and confinement, we studied urokinase plasminogen activator (uPA) receptor (uPAR), a GPI receptor involved in the regulation of cell adhesion, migration, and proliferatio...

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Autores principales: Caiolfa, Valeria R., Zamai, Moreno, Malengo, Gabriele, Andolfo, Annapaola, Madsen, Chris D., Sutin, Jason, Digman, Michelle A., Gratton, Enrico, Blasi, Francesco, Sidenius, Nicolai
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 2007
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2099195/
https://www.ncbi.nlm.nih.gov/pubmed/18056417
http://dx.doi.org/10.1083/jcb.200702151
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author Caiolfa, Valeria R.
Zamai, Moreno
Malengo, Gabriele
Andolfo, Annapaola
Madsen, Chris D.
Sutin, Jason
Digman, Michelle A.
Gratton, Enrico
Blasi, Francesco
Sidenius, Nicolai
author_facet Caiolfa, Valeria R.
Zamai, Moreno
Malengo, Gabriele
Andolfo, Annapaola
Madsen, Chris D.
Sutin, Jason
Digman, Michelle A.
Gratton, Enrico
Blasi, Francesco
Sidenius, Nicolai
author_sort Caiolfa, Valeria R.
collection PubMed
description To search for functional links between glycosylphosphatidylinositol (GPI) protein monomer–oligomer exchange and membrane dynamics and confinement, we studied urokinase plasminogen activator (uPA) receptor (uPAR), a GPI receptor involved in the regulation of cell adhesion, migration, and proliferation. Using a functionally active fluorescent protein–uPAR in live cells, we analyzed the effect that extracellular matrix proteins and uPAR ligands have on uPAR dynamics and dimerization at the cell membrane. Vitronectin directs the recruitment of dimers and slows down the diffusion of the receptors at the basal membrane. The commitment to uPA–plasminogen activator inhibitor type 1–mediated endocytosis and recycling modifies uPAR diffusion and induces an exchange between uPAR monomers and dimers. This exchange is fully reversible. The data demonstrate that cell surface protein assemblies are important in regulating the dynamics and localization of uPAR at the cell membrane and the exchange of monomers and dimers. These results also provide a strong rationale for dynamic studies of GPI-anchored molecules in live cells at steady state and in the absence of cross-linker/clustering agents.
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spelling pubmed-20991952008-06-03 Monomer–dimer dynamics and distribution of GPI-anchored uPAR are determined by cell surface protein assemblies Caiolfa, Valeria R. Zamai, Moreno Malengo, Gabriele Andolfo, Annapaola Madsen, Chris D. Sutin, Jason Digman, Michelle A. Gratton, Enrico Blasi, Francesco Sidenius, Nicolai J Cell Biol Research Articles To search for functional links between glycosylphosphatidylinositol (GPI) protein monomer–oligomer exchange and membrane dynamics and confinement, we studied urokinase plasminogen activator (uPA) receptor (uPAR), a GPI receptor involved in the regulation of cell adhesion, migration, and proliferation. Using a functionally active fluorescent protein–uPAR in live cells, we analyzed the effect that extracellular matrix proteins and uPAR ligands have on uPAR dynamics and dimerization at the cell membrane. Vitronectin directs the recruitment of dimers and slows down the diffusion of the receptors at the basal membrane. The commitment to uPA–plasminogen activator inhibitor type 1–mediated endocytosis and recycling modifies uPAR diffusion and induces an exchange between uPAR monomers and dimers. This exchange is fully reversible. The data demonstrate that cell surface protein assemblies are important in regulating the dynamics and localization of uPAR at the cell membrane and the exchange of monomers and dimers. These results also provide a strong rationale for dynamic studies of GPI-anchored molecules in live cells at steady state and in the absence of cross-linker/clustering agents. The Rockefeller University Press 2007-12-03 /pmc/articles/PMC2099195/ /pubmed/18056417 http://dx.doi.org/10.1083/jcb.200702151 Text en Copyright © 2007, 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
Caiolfa, Valeria R.
Zamai, Moreno
Malengo, Gabriele
Andolfo, Annapaola
Madsen, Chris D.
Sutin, Jason
Digman, Michelle A.
Gratton, Enrico
Blasi, Francesco
Sidenius, Nicolai
Monomer–dimer dynamics and distribution of GPI-anchored uPAR are determined by cell surface protein assemblies
title Monomer–dimer dynamics and distribution of GPI-anchored uPAR are determined by cell surface protein assemblies
title_full Monomer–dimer dynamics and distribution of GPI-anchored uPAR are determined by cell surface protein assemblies
title_fullStr Monomer–dimer dynamics and distribution of GPI-anchored uPAR are determined by cell surface protein assemblies
title_full_unstemmed Monomer–dimer dynamics and distribution of GPI-anchored uPAR are determined by cell surface protein assemblies
title_short Monomer–dimer dynamics and distribution of GPI-anchored uPAR are determined by cell surface protein assemblies
title_sort monomer–dimer dynamics and distribution of gpi-anchored upar are determined by cell surface protein assemblies
topic Research Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2099195/
https://www.ncbi.nlm.nih.gov/pubmed/18056417
http://dx.doi.org/10.1083/jcb.200702151
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