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Lauwers, E., Wang, Y.C., Gallardo, R., Van der Kant, R., Michiels, E., Swerts, J., Baatsen, P., Zaiter, S.S., McAlpine, S.R., Gounko, N.V., Rousseau, F., Schymkowitz, J., Verstreken, P. (2018). Hsp90 Mediates Membrane Deformation and Exosome Release.  Mol. Cell 71(5): 689--702.e9.
FlyBase ID
FBrf0241927
Publication Type
Research paper
Abstract

Hsp90 is an essential chaperone that guards proteome integrity and amounts to 2% of cellular protein. We now find that Hsp90 also has the ability to directly interact with and deform membranes via an evolutionarily conserved amphipathic helix. Using a new cell-free system and in vivo measurements, we show this amphipathic helix allows exosome release by promoting the fusion of multivesicular bodies (MVBs) with the plasma membrane. We dissect the relationship between Hsp90 conformation and membrane-deforming function and show that mutations and drugs that stabilize the open Hsp90 dimer expose the helix and allow MVB fusion, while these effects are blocked by the closed state. Hence, we structurally separated the Hsp90 membrane-deforming function from its well-characterized chaperone activity, and we show that this previously unrecognized function is required for exosome release.

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    Language of Publication
    English
    Additional Languages of Abstract
    Parent Publication
    Publication Type
    Journal
    Abbreviation
    Mol. Cell
    Title
    Molecular Cell
    Publication Year
    1997-
    ISBN/ISSN
    1097-2765 1097-4164
    Data From Reference
    Genes (4)
    Cell Lines (1)