 |
Journal articles
Interaction of the chaperones alpha B-crystallin and CHIP with fibrillar alpha-synuclein: Effects on internalization by cells and identification of interacting interfaces
Abstract : The spread of fibrillar alpha-synuclein from affected to naïve neuronal cells is thought to contribute to the progression of synucleinopathies. The binding of fibrillar alpha-synuclein to the plasma membrane is key in this process. We and others previously showed that coating fibrillar alpha-synuclein by the molecular chaperone Hsc70 affects fibrils properties. Here we assessed the effect of the two molecular chaperones alpha B-crystallin and CHIP on alpha-synuclein fibrils uptake by Neuro-2a cells. We demonstrate that both chaperones diminish fibrils take up by cells. We identify through a cross-linking and mass spectrometry strategy the interaction interfaces between alpha-synuclein fibrils and alpha B-crystallin or CHIP. Our results open the way for designing chaperone-derived polypeptide binders that interfere with the propagation of pathogenic alpha-synuclein assemblies.
Cited literature [62 references]
https://hal-cea.archives-ouvertes.fr/cea-02614589
Contributor : Mehdi Kabani <>
Submitted on : Thursday, May 21, 2020 - 11:10:57 AM
Last modification on : Friday, July 2, 2021 - 3:45:58 AM
Contributor : Mehdi Kabani <>
Submitted on : Thursday, May 21, 2020 - 11:10:57 AM
Last modification on : Friday, July 2, 2021 - 3:45:58 AM
File
2020_aSyn_ABC_CHIP_Bendifallah...
Publisher files allowed on an open archive