The intracellular translocation of the components of the fibroblast growth factor 1 release complex precedes their assembly prior to export
| Autor: | Igor Prudovsky, Stephen Bellum, Francesca Tarantini, Cinzia Bagalà, Anna Mandinova, Thomas Maciag, Raffaella Soldi |
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| Rok vydání: | 2002 |
| Předmět: |
Stress fiber
Nerve Tissue Proteins Biology Synaptotagmin 1 Mice Synaptotagmins 03 medical and health sciences 0302 clinical medicine Report Animals fibroblast growth factor heat shock S100A13 Synaptotagmin1 confocal microscopy Cytoskeleton 030304 developmental biology 0303 health sciences Membrane Glycoproteins Microscopy Confocal Calcium-Binding Proteins S100 Proteins Synaptotagmin I 3T3 Cells Intracellular Membranes Cell Biology FGF1 Transport protein Cell biology Protein Transport Cytosol 030220 oncology & carcinogenesis Fibroblast Growth Factor 1 Intracellular Protein Binding |
| Zdroj: | The Journal of Cell Biology |
| ISSN: | 1540-8140 0021-9525 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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