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Single event visualization of unconventional secretion of FGF2

FGF2 is exported from cells by an unconventional secretory mechanism. Here, we directly visualized individual FGF2 membrane translocation events at the plasma membrane using live cell TIRF microscopy. This process was dependent on both PI(4,5)P2-mediated recruitment of FGF2 at the inner leaflet and...

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Bibliographic Details
Main Authors: Dimou, Eleni (Author) , Katsinelos, Taxiarchis (Author) , Wegehingel, Sabine (Author) , Nickel, Walter (Author)
Format: Article (Journal)
Language:English
Published: 2019
In: The journal of cell biology
Year: 2018, Volume: 218, Issue: 2, Pages: 683-699
ISSN:1540-8140
DOI:10.1083/jcb.201802008
Online Access:Verlag, Volltext: https://doi.org/10.1083/jcb.201802008
Verlag: http://jcb.rupress.org/content/218/2/683
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Author Notes:Eleni Dimou, Katia Cosentino, Evgenia Platonova, Uris Ros, Mohsen Sadeghi, Purba Kashyap, Taxiarchis Katsinelos, Sabine Wegehingel, Frank Noé, Ana J. García-Sáez, Helge Ewers, and Walter Nickel
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Summary:FGF2 is exported from cells by an unconventional secretory mechanism. Here, we directly visualized individual FGF2 membrane translocation events at the plasma membrane using live cell TIRF microscopy. This process was dependent on both PI(4,5)P2-mediated recruitment of FGF2 at the inner leaflet and heparan sulfates capturing FGF2 at the outer plasma membrane leaflet. By simultaneous imaging of both FGF2 membrane recruitment and the appearance of FGF2 at the cell surface, we revealed the kinetics of FGF2 membrane translocation in living cells with an average duration of ∼200 ms. Furthermore, we directly demonstrated FGF2 oligomers at the inner leaflet of living cells with a FGF2 dimer being the most prominent species. We propose this dimer to represent a key intermediate in the formation of higher FGF2 oligomers that form membrane pores and put forward a kinetic model explaining the mechanism by which membrane-inserted FGF2 oligomers serve as dynamic translocation intermediates during unconventional secretion of FGF2.
Item Description:Published online: 23 November, 2018
Gesehen am 30.10.2019
Physical Description:Online Resource
ISSN:1540-8140
DOI:10.1083/jcb.201802008

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