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Oligomerization of expanded-polyglutamine domain fluorescent fusion proteins in cultured mammalian cells.

Publication ,  Journal Article
Onodera, O; Burke, JR; Miller, SE; Hester, S; Tsuji, S; Roses, AD; Strittmatter, WJ
Published in: Biochem Biophys Res Commun
September 18, 1997

Six inherited neurologic diseases, including Huntington's disease, result from the expansion of a CAG domain of the disease genes to produce a domain of more than 40 glutamines in the expressed protein. The mechanism by which expansion of this polyglutamine domain causes disease is unknown. Recent studies demonstrated oligomerization of polyglutamine-domain proteins in mammalian neurons. To study oligomerization of polyglutamine proteins and to identify heterologous protein interactions, varying length polyglutamine-green fluorescent protein fusion proteins were expressed in cultured COS-7 cells. The 19- and 35-glutamine fusion proteins (non-pathologic length) distributed diffusely throughout the cytoplasm. In contrast, 56- and 80-glutamine fusion proteins (pathologic length) formed fibrillar arrays resembling those previously observed in neurons in Huntington's disease and in a transgenic mouse model. These aggregates were intranuclear and intracytoplasmic. Intracytoplasmic aggregates were surrounded by collapsed intermediate filaments. The intermediate filament protein vimentin co-immunoisolated with expanded polyglutamine fusion proteins. This cellular model will expedite investigations into oligomerization of polyglutamine proteins and their interactions with other proteins.

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Published In

Biochem Biophys Res Commun

DOI

ISSN

0006-291X

Publication Date

September 18, 1997

Volume

238

Issue

2

Start / End Page

599 / 605

Location

United States

Related Subject Headings

  • Recombinant Fusion Proteins
  • Peptides
  • Mice
  • Luminescent Proteins
  • Green Fluorescent Proteins
  • Dimerization
  • COS Cells
  • Biochemistry & Molecular Biology
  • Animals
  • 3404 Medicinal and biomolecular chemistry
 

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Onodera, O., Burke, J. R., Miller, S. E., Hester, S., Tsuji, S., Roses, A. D., & Strittmatter, W. J. (1997). Oligomerization of expanded-polyglutamine domain fluorescent fusion proteins in cultured mammalian cells. Biochem Biophys Res Commun, 238(2), 599–605. https://doi.org/10.1006/bbrc.1997.7337
Onodera, O., J. R. Burke, S. E. Miller, S. Hester, S. Tsuji, A. D. Roses, and W. J. Strittmatter. “Oligomerization of expanded-polyglutamine domain fluorescent fusion proteins in cultured mammalian cells.Biochem Biophys Res Commun 238, no. 2 (September 18, 1997): 599–605. https://doi.org/10.1006/bbrc.1997.7337.
Onodera O, Burke JR, Miller SE, Hester S, Tsuji S, Roses AD, et al. Oligomerization of expanded-polyglutamine domain fluorescent fusion proteins in cultured mammalian cells. Biochem Biophys Res Commun. 1997 Sep 18;238(2):599–605.
Onodera, O., et al. “Oligomerization of expanded-polyglutamine domain fluorescent fusion proteins in cultured mammalian cells.Biochem Biophys Res Commun, vol. 238, no. 2, Sept. 1997, pp. 599–605. Pubmed, doi:10.1006/bbrc.1997.7337.
Onodera O, Burke JR, Miller SE, Hester S, Tsuji S, Roses AD, Strittmatter WJ. Oligomerization of expanded-polyglutamine domain fluorescent fusion proteins in cultured mammalian cells. Biochem Biophys Res Commun. 1997 Sep 18;238(2):599–605.
Journal cover image

Published In

Biochem Biophys Res Commun

DOI

ISSN

0006-291X

Publication Date

September 18, 1997

Volume

238

Issue

2

Start / End Page

599 / 605

Location

United States

Related Subject Headings

  • Recombinant Fusion Proteins
  • Peptides
  • Mice
  • Luminescent Proteins
  • Green Fluorescent Proteins
  • Dimerization
  • COS Cells
  • Biochemistry & Molecular Biology
  • Animals
  • 3404 Medicinal and biomolecular chemistry