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Tau induces formation of α-synuclein filaments with distinct molecular conformations.

Publication ,  Journal Article
Hojjatian, A; Dasari, AKR; Sengupta, U; Taylor, D; Daneshparvar, N; Yeganeh, FA; Dillard, L; Michael, B; Griffin, RG; Borgnia, MJ; Kayed, R ...
Published in: Biochem Biophys Res Commun
May 21, 2021

Recent structural investigation of amyloid filaments extracted from human patients demonstrated that the ex vivo filaments associated with different disease phenotypes adopt diverse molecular conformations, which are different from those of in vitro amyloid filaments. A very recent cryo-EM structural study also revealed that ex vivo α-synuclein filaments extracted from multiple system atrophy patients adopt distinct molecular structures from those of in vitro α-synuclein filaments, suggesting the presence of co-factors for α-synuclein aggregation in vivo. Here, we report structural characterizations of α-synuclein filaments formed in the presence of a potential co-factor, tau, using cryo-EM and solid-state NMR. Our cryo-EM structure of the tau-promoted α-synuclein filaments reveals some similarities to one of the previously reported polymorphs of in vitro α-synuclein filaments in the core region, while illustrating distinct conformations in the N- and C-terminal regions. The structural study highlights the conformational plasticity of α-synuclein filaments and the importance of the co-factors, requiring additional structural investigation of not only more ex vivo α-synuclein filaments, but also in vitro α-synuclein filaments formed in the presence of diverse co-factors. The comparative structural analyses will help better understand molecular basis of diverse structures of α-synuclein filaments and possible relevance of each structure to the disease phenotype.

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Published In

Biochem Biophys Res Commun

DOI

EISSN

1090-2104

Publication Date

May 21, 2021

Volume

554

Start / End Page

145 / 150

Location

United States

Related Subject Headings

  • tau Proteins
  • alpha-Synuclein
  • Recombinant Proteins
  • Protein Conformation
  • Microscopy, Immunoelectron
  • Magnetic Resonance Spectroscopy
  • Humans
  • Cryoelectron Microscopy
  • Brain Chemistry
  • Brain
 

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Hojjatian, A., Dasari, A. K. R., Sengupta, U., Taylor, D., Daneshparvar, N., Yeganeh, F. A., … Lim, K. H. (2021). Tau induces formation of α-synuclein filaments with distinct molecular conformations. Biochem Biophys Res Commun, 554, 145–150. https://doi.org/10.1016/j.bbrc.2021.03.091
Hojjatian, Alimohammad, Anvesh K. R. Dasari, Urmi Sengupta, Dianne Taylor, Nadia Daneshparvar, Fatemeh Abbasi Yeganeh, Lucas Dillard, et al. “Tau induces formation of α-synuclein filaments with distinct molecular conformations.Biochem Biophys Res Commun 554 (May 21, 2021): 145–50. https://doi.org/10.1016/j.bbrc.2021.03.091.
Hojjatian A, Dasari AKR, Sengupta U, Taylor D, Daneshparvar N, Yeganeh FA, et al. Tau induces formation of α-synuclein filaments with distinct molecular conformations. Biochem Biophys Res Commun. 2021 May 21;554:145–50.
Hojjatian, Alimohammad, et al. “Tau induces formation of α-synuclein filaments with distinct molecular conformations.Biochem Biophys Res Commun, vol. 554, May 2021, pp. 145–50. Pubmed, doi:10.1016/j.bbrc.2021.03.091.
Hojjatian A, Dasari AKR, Sengupta U, Taylor D, Daneshparvar N, Yeganeh FA, Dillard L, Michael B, Griffin RG, Borgnia MJ, Kayed R, Taylor KA, Lim KH. Tau induces formation of α-synuclein filaments with distinct molecular conformations. Biochem Biophys Res Commun. 2021 May 21;554:145–150.
Journal cover image

Published In

Biochem Biophys Res Commun

DOI

EISSN

1090-2104

Publication Date

May 21, 2021

Volume

554

Start / End Page

145 / 150

Location

United States

Related Subject Headings

  • tau Proteins
  • alpha-Synuclein
  • Recombinant Proteins
  • Protein Conformation
  • Microscopy, Immunoelectron
  • Magnetic Resonance Spectroscopy
  • Humans
  • Cryoelectron Microscopy
  • Brain Chemistry
  • Brain