SwePub
Sök i LIBRIS databas

  Extended search

onr:"swepub:oai:research.chalmers.se:074c70ea-5a29-49b7-be3c-f3173faee648"
 

Search: onr:"swepub:oai:research.chalmers.se:074c70ea-5a29-49b7-be3c-f3173faee648" > Interaction between...

  • 1 of 1
  • Previous record
  • Next record
  •    To hitlist
  • Horvath, Istvan,1979Chalmers tekniska högskola,Chalmers University of Technology (author)

Interaction between Copper Chaperone Atox1 and Parkinson's Disease Protein α-Synuclein Includes Metal-Binding Sites and Occurs in Living Cells

  • Article/chapterEnglish2019

Publisher, publication year, extent ...

  • 2019-10-10
  • American Chemical Society (ACS),2019

Numbers

  • LIBRIS-ID:oai:research.chalmers.se:074c70ea-5a29-49b7-be3c-f3173faee648
  • https://research.chalmers.se/publication/513667URI
  • https://doi.org/10.1021/acschemneuro.9b00476DOI

Supplementary language notes

  • Language:English
  • Summary in:English

Part of subdatabase

Classification

  • Subject category:art swepub-publicationtype
  • Subject category:ref swepub-contenttype

Notes

  • Alterations in copper ion homeostasis appear coupled to neurodegenerative disorders, but mechanisms are unknown. The cytoplasmic copper chaperone Atox1 was recently found to inhibit amyloid formation in vitro of α-synuclein, the amyloidogenic protein in Parkinson's disease. As α-synuclein may have copper-dependent functions, and free copper ions promote α-synuclein amyloid formation, it is important to characterize the Atox1 interaction with α-synuclein on a molecular level. Here we applied solution-state nuclear magnetic resonance spectroscopy, with isotopically labeled α-synuclein and Atox1, to define interaction regions in both proteins. The α-synuclein interaction interface includes the whole N-terminal part up to Gln24; in Atox1, residues around the copper-binding cysteines (positions 11-16) are mostly perturbed, but additional effects are also found for residues elsewhere in both proteins. Because α-synuclein is N-terminally acetylated in vivo, we established that Atox1 also inhibits amyloid formation of this variant in vitro, and proximity ligation in human cell lines demonstrated α-synuclein-Atox1 interactions in situ. Thus, this interaction may provide the direct link between copper homeostasis and amyloid formation in vivo.

Subject headings and genre

Added entries (persons, corporate bodies, meetings, titles ...)

  • Blockhuys, Stephanie,1983Chalmers tekniska högskola,Chalmers University of Technology(Swepub:cth)steblo (author)
  • Šulskis, DariusGöteborgs universitet,University of Gothenburg (author)
  • Holgersson, Stellan,1964Chalmers tekniska högskola,Chalmers University of Technology(Swepub:cth)stehol (author)
  • Kumar, Ranjeet,1980Chalmers tekniska högskola,Chalmers University of Technology(Swepub:cth)ranjeet (author)
  • Burmann, Björn M.Göteborgs universitet,University of Gothenburg (author)
  • Wittung Stafshede, Pernilla,1968Chalmers tekniska högskola,Chalmers University of Technology(Swepub:cth)perwit (author)
  • Chalmers tekniska högskolaGöteborgs universitet (creator_code:org_t)

Related titles

  • In:ACS Chemical Neuroscience: American Chemical Society (ACS)10:11, s. 4659-46681948-7193

Internet link

Find in a library

To the university's database

  • 1 of 1
  • Previous record
  • Next record
  •    To hitlist

Kungliga biblioteket hanterar dina personuppgifter i enlighet med EU:s dataskyddsförordning (2018), GDPR. Läs mer om hur det funkar här.
Så här hanterar KB dina uppgifter vid användning av denna tjänst.

 
pil uppåt Close

Copy and save the link in order to return to this view