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Pregled bibliografske jedinice broj: 1127952

α-synuclein oligomers interact with ATP synthase and open the permeability transition pore in Parkinson’s disease

Ludtmann, Marthe H. R.; Angelova, Plamena R.; Horrocks, Mathew H.; Choi, Minee L.; Rodrigues, Margarida; Baev, Artyom Y.; Berezhnov, Alexey V.; Yao, Zhi; Little, Daniel; Banushi, Blerida et al.
α-synuclein oligomers interact with ATP synthase and open the permeability transition pore in Parkinson’s disease // Nature communications, 9 (2018), 1; 2293, 16 doi:10.1038/s41467-018-04422-2 (međunarodna recenzija, članak, znanstveni)

CROSBI ID: 1127952 Za ispravke kontaktirajte CROSBI podršku putem web obrasca

Naslov
α-synuclein oligomers interact with ATP synthase and open the permeability transition pore in Parkinson’s disease

Autori
Ludtmann, Marthe H. R. ; Angelova, Plamena R. ; Horrocks, Mathew H. ; Choi, Minee L. ; Rodrigues, Margarida ; Baev, Artyom Y. ; Berezhnov, Alexey V. ; Yao, Zhi ; Little, Daniel ; Banushi, Blerida ; Al-Menhali, Afnan Saleh ; Ranasinghe, Rohan T. ; Whiten, Daniel R. ; Yapom, Ratsuda ; Dolt, Karamjit Singh ; Devine, Michael J. ; Gissen, Paul ; Kunath, Tilo ; Jaganjac, Morana ; Pavlov, Evgeny V. ; Klenerman, David ; Abramov, Andrey Y. ; Gandhi, Sonia

Izvornik
Nature communications (2041-1723) 9 (2018), 1; 2293, 16

Vrsta, podvrsta i kategorija rada
Radovi u časopisima, članak, znanstveni

Ključne riječi
α-synuclein ; ATP synthase ; Parkinson’s disease

Sažetak
Protein aggregation causes α-synuclein to switch from its physiological role to a pathological toxic gain of function. Under physiological conditions, monomeric α-synuclein improves ATP synthase efficiency. Here, we report that aggregation of monomers generates beta sheet-rich oligomers that localise to the mitochondria in close proximity to several mitochondrial proteins including ATP synthase. Oligomeric α-synuclein impairs complex I- dependent respiration. Oligomers induce selective oxidation of the ATP synthase beta subunit and mitochondrial lipid peroxidation. These oxidation events increase the probability of permeability transition pore (PTP) opening, triggering mitochondrial swelling, and ultimately cell death. Notably, inhibition of oligomer-induced oxidation prevents the pathological induction of PTP. Inducible pluripotent stem cells (iPSC)-derived neurons bearing SNCA triplication, generate α-synuclein aggregates that interact with the ATP synthase and induce PTP opening, leading to neuronal death. This study shows how the transition of α-synuclein from its monomeric to oligomeric structure alters its functional consequences in Parkinson's disease.

Izvorni jezik
Engleski

Znanstvena područja
Temeljne medicinske znanosti



POVEZANOST RADA

Profili:

Avatar Url Morana Jaganjac (autor)

Poveznice na cjeloviti tekst rada:

doi www.nature.com

Citiraj ovu publikaciju:

Ludtmann, Marthe H. R.; Angelova, Plamena R.; Horrocks, Mathew H.; Choi, Minee L.; Rodrigues, Margarida; Baev, Artyom Y.; Berezhnov, Alexey V.; Yao, Zhi; Little, Daniel; Banushi, Blerida et al.
α-synuclein oligomers interact with ATP synthase and open the permeability transition pore in Parkinson’s disease // Nature communications, 9 (2018), 1; 2293, 16 doi:10.1038/s41467-018-04422-2 (međunarodna recenzija, članak, znanstveni)
Ludtmann, M., Angelova, P., Horrocks, M., Choi, M., Rodrigues, M., Baev, A., Berezhnov, A., Yao, Z., Little, D. & Banushi, B. (2018) α-synuclein oligomers interact with ATP synthase and open the permeability transition pore in Parkinson’s disease. Nature communications, 9 (1), 2293, 16 doi:10.1038/s41467-018-04422-2.
@article{article, author = {Ludtmann, Marthe H. R. and Angelova, Plamena R. and Horrocks, Mathew H. and Choi, Minee L. and Rodrigues, Margarida and Baev, Artyom Y. and Berezhnov, Alexey V. and Yao, Zhi and Little, Daniel and Banushi, Blerida and Al-Menhali, Afnan Saleh and Ranasinghe, Rohan T. and Whiten, Daniel R. and Yapom, Ratsuda and Dolt, Karamjit Singh and Devine, Michael J. and Gissen, Paul and Kunath, Tilo and Jaganjac, Morana and Pavlov, Evgeny V. and Klenerman, David and Abramov, Andrey Y. and Gandhi, Sonia}, year = {2018}, pages = {16}, DOI = {10.1038/s41467-018-04422-2}, chapter = {2293}, keywords = {α-synuclein, ATP synthase, Parkinson’s disease}, journal = {Nature communications}, doi = {10.1038/s41467-018-04422-2}, volume = {9}, number = {1}, issn = {2041-1723}, title = {α-synuclein oligomers interact with ATP synthase and open the permeability transition pore in Parkinson’s disease}, keyword = {α-synuclein, ATP synthase, Parkinson’s disease}, chapternumber = {2293} }
@article{article, author = {Ludtmann, Marthe H. R. and Angelova, Plamena R. and Horrocks, Mathew H. and Choi, Minee L. and Rodrigues, Margarida and Baev, Artyom Y. and Berezhnov, Alexey V. and Yao, Zhi and Little, Daniel and Banushi, Blerida and Al-Menhali, Afnan Saleh and Ranasinghe, Rohan T. and Whiten, Daniel R. and Yapom, Ratsuda and Dolt, Karamjit Singh and Devine, Michael J. and Gissen, Paul and Kunath, Tilo and Jaganjac, Morana and Pavlov, Evgeny V. and Klenerman, David and Abramov, Andrey Y. and Gandhi, Sonia}, year = {2018}, pages = {16}, DOI = {10.1038/s41467-018-04422-2}, chapter = {2293}, keywords = {α-synuclein, ATP synthase, Parkinson’s disease}, journal = {Nature communications}, doi = {10.1038/s41467-018-04422-2}, volume = {9}, number = {1}, issn = {2041-1723}, title = {α-synuclein oligomers interact with ATP synthase and open the permeability transition pore in Parkinson’s disease}, keyword = {α-synuclein, ATP synthase, Parkinson’s disease}, chapternumber = {2293} }

Časopis indeksira:


  • Current Contents Connect (CCC)
  • Web of Science Core Collection (WoSCC)
    • Science Citation Index Expanded (SCI-EXP)
    • SCI-EXP, SSCI i/ili A&HCI
  • Scopus
  • MEDLINE
  • Nature Index

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