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The intracellular translocation of the components of the fibroblast growth factor 1 release complex precedes their assembly prior to export
The release of signal peptideless proteins occurs through nonclassical export pathways and the release of fibroblast growth factor (FGF)1 in response to cellular stress is well documented. Although biochemical evidence suggests that the formation of a multiprotein complex containing S100A13 and Syna...
Autores principales: | , , , , , , |
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Formato: | Texto |
Lenguaje: | English |
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The Rockefeller University Press
2002
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2173119/ https://www.ncbi.nlm.nih.gov/pubmed/12135982 http://dx.doi.org/10.1083/jcb.200203084 |
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author | Prudovsky, Igor Bagala, Cinzia Tarantini, Francesca Mandinova, Anna Soldi, Raffaella Bellum, Stephen Maciag, Thomas |
author_facet | Prudovsky, Igor Bagala, Cinzia Tarantini, Francesca Mandinova, Anna Soldi, Raffaella Bellum, Stephen Maciag, Thomas |
author_sort | Prudovsky, Igor |
collection | PubMed |
description | The release of signal peptideless proteins occurs through nonclassical export pathways and the release of fibroblast growth factor (FGF)1 in response to cellular stress is well documented. Although biochemical evidence suggests that the formation of a multiprotein complex containing S100A13 and Synaptotagmin (Syt)1 is important for the release of FGF1, it is unclear where this intracellular complex is assembled. As a result, we employed real-time analysis using confocal fluorescence microscopy to study the spatio-temporal aspects of this nonclassical export pathway and demonstrate that heat shock stimulates the redistribution of FGF1 from a diffuse cytosolic pattern to a locale near the inner surface of the plasma membrane where it colocalized with S100A13 and Syt1. In addition, coexpression of dominant-negative mutant forms of S100A13 and Syt1, which both repress the release of FGF1, failed to inhibit the stress-induced peripheral redistribution of intracellular FGF1. However, amlexanox, a compound that is known to attenuate actin stress fiber formation and FGF1 release, was able to repress this process. These data suggest that the assembly of the intracellular complex involved in the release of FGF1 occurs near the inner surface of the plasma membrane and is dependent on the F-actin cytoskeleton. |
format | Text |
id | pubmed-2173119 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2002 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-21731192008-05-01 The intracellular translocation of the components of the fibroblast growth factor 1 release complex precedes their assembly prior to export Prudovsky, Igor Bagala, Cinzia Tarantini, Francesca Mandinova, Anna Soldi, Raffaella Bellum, Stephen Maciag, Thomas J Cell Biol Report The release of signal peptideless proteins occurs through nonclassical export pathways and the release of fibroblast growth factor (FGF)1 in response to cellular stress is well documented. Although biochemical evidence suggests that the formation of a multiprotein complex containing S100A13 and Synaptotagmin (Syt)1 is important for the release of FGF1, it is unclear where this intracellular complex is assembled. As a result, we employed real-time analysis using confocal fluorescence microscopy to study the spatio-temporal aspects of this nonclassical export pathway and demonstrate that heat shock stimulates the redistribution of FGF1 from a diffuse cytosolic pattern to a locale near the inner surface of the plasma membrane where it colocalized with S100A13 and Syt1. In addition, coexpression of dominant-negative mutant forms of S100A13 and Syt1, which both repress the release of FGF1, failed to inhibit the stress-induced peripheral redistribution of intracellular FGF1. However, amlexanox, a compound that is known to attenuate actin stress fiber formation and FGF1 release, was able to repress this process. These data suggest that the assembly of the intracellular complex involved in the release of FGF1 occurs near the inner surface of the plasma membrane and is dependent on the F-actin cytoskeleton. The Rockefeller University Press 2002-07-22 /pmc/articles/PMC2173119/ /pubmed/12135982 http://dx.doi.org/10.1083/jcb.200203084 Text en Copyright © 2002, 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 | Report Prudovsky, Igor Bagala, Cinzia Tarantini, Francesca Mandinova, Anna Soldi, Raffaella Bellum, Stephen Maciag, Thomas The intracellular translocation of the components of the fibroblast growth factor 1 release complex precedes their assembly prior to export |
title | The intracellular translocation of the components of the fibroblast growth factor 1 release complex precedes their assembly prior to export |
title_full | The intracellular translocation of the components of the fibroblast growth factor 1 release complex precedes their assembly prior to export |
title_fullStr | The intracellular translocation of the components of the fibroblast growth factor 1 release complex precedes their assembly prior to export |
title_full_unstemmed | The intracellular translocation of the components of the fibroblast growth factor 1 release complex precedes their assembly prior to export |
title_short | The intracellular translocation of the components of the fibroblast growth factor 1 release complex precedes their assembly prior to export |
title_sort | intracellular translocation of the components of the fibroblast growth factor 1 release complex precedes their assembly prior to export |
topic | Report |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2173119/ https://www.ncbi.nlm.nih.gov/pubmed/12135982 http://dx.doi.org/10.1083/jcb.200203084 |
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