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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...

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Detalles Bibliográficos
Autores principales: Prudovsky, Igor, Bagala, Cinzia, Tarantini, Francesca, Mandinova, Anna, Soldi, Raffaella, Bellum, Stephen, Maciag, Thomas
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 2002
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.
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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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