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Caveolin-1: an ambiguous partner in cell signalling and cancer

Caveolae are small plasma membrane invaginations that have been implicated in a variety of functions including transcytosis, potocytosis and cholesterol transport and signal transduction. The major protein component of this compartment is a family of proteins called caveolins. Experimental data obta...

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Detalles Bibliográficos
Autores principales: Quest, Andrew F G, Gutierrez-Pajares, Jorge L, Torres, Vicente A
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Blackwell Publishing Ltd 2008
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3865655/
https://www.ncbi.nlm.nih.gov/pubmed/18400052
http://dx.doi.org/10.1111/j.1582-4934.2008.00331.x
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author Quest, Andrew F G
Gutierrez-Pajares, Jorge L
Torres, Vicente A
author_facet Quest, Andrew F G
Gutierrez-Pajares, Jorge L
Torres, Vicente A
author_sort Quest, Andrew F G
collection PubMed
description Caveolae are small plasma membrane invaginations that have been implicated in a variety of functions including transcytosis, potocytosis and cholesterol transport and signal transduction. The major protein component of this compartment is a family of proteins called caveolins. Experimental data obtained in knockout mice have provided unequivocal evidence for a requirement of caveolins to generate morphologically detectable caveolae structures. However, expression of caveolins is not sufficient per seto assure the presence of these structures. With respect to other roles attributed to caveolins in the regulation of cellular function, insights are even less clear. Here we will consider, more specifically, the data concerning the ambiguous roles ascribed to caveolin-1 in signal transduction and cancer. In particular, evidence indicating that caveolin-1 function is cell context dependent will be discussed.
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spelling pubmed-38656552015-04-27 Caveolin-1: an ambiguous partner in cell signalling and cancer Quest, Andrew F G Gutierrez-Pajares, Jorge L Torres, Vicente A J Cell Mol Med Reviews Caveolae are small plasma membrane invaginations that have been implicated in a variety of functions including transcytosis, potocytosis and cholesterol transport and signal transduction. The major protein component of this compartment is a family of proteins called caveolins. Experimental data obtained in knockout mice have provided unequivocal evidence for a requirement of caveolins to generate morphologically detectable caveolae structures. However, expression of caveolins is not sufficient per seto assure the presence of these structures. With respect to other roles attributed to caveolins in the regulation of cellular function, insights are even less clear. Here we will consider, more specifically, the data concerning the ambiguous roles ascribed to caveolin-1 in signal transduction and cancer. In particular, evidence indicating that caveolin-1 function is cell context dependent will be discussed. Blackwell Publishing Ltd 2008-08 2008-04-08 /pmc/articles/PMC3865655/ /pubmed/18400052 http://dx.doi.org/10.1111/j.1582-4934.2008.00331.x Text en © 2008 The Authors Journal compilation © 2008 Foundation for Cellular and Molecular Medicine/Blackwell Publishing Ltd http://creativecommons.org/licenses/by/2.5/ Re-use of this article is permitted in accordance with the Creative Commons Deed, Attribution 2.5, which does not permit commercial exploitation.
spellingShingle Reviews
Quest, Andrew F G
Gutierrez-Pajares, Jorge L
Torres, Vicente A
Caveolin-1: an ambiguous partner in cell signalling and cancer
title Caveolin-1: an ambiguous partner in cell signalling and cancer
title_full Caveolin-1: an ambiguous partner in cell signalling and cancer
title_fullStr Caveolin-1: an ambiguous partner in cell signalling and cancer
title_full_unstemmed Caveolin-1: an ambiguous partner in cell signalling and cancer
title_short Caveolin-1: an ambiguous partner in cell signalling and cancer
title_sort caveolin-1: an ambiguous partner in cell signalling and cancer
topic Reviews
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3865655/
https://www.ncbi.nlm.nih.gov/pubmed/18400052
http://dx.doi.org/10.1111/j.1582-4934.2008.00331.x
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