The intracellular translocation of the components of the fibroblast growth factor 1 release complex precedes their assembly prior to export.

ABSTRACT: 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, coexpressi

SUBMITTER: Prudovsky I 

PROVIDER: S-EPMC2173119 | biostudies-literature | 2002 Jul

REPOSITORIES: biostudies-literature