Targeting Expression of Expanded Polyglutamine Proteins to the Endoplasmic Reticulum or Mitochondria Prevents Their Aggregation

Aggregation of misfolded proteins is a characteristic of several neurodegenerative diseases. The huntingtin amino-terminal fragment with extended polyglutamine repeat forms aggregates closely associated with chaperones both in the cytoplasm and the nucleus. Because each cellular compartment contains...

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Veröffentlicht in:	Proceedings of the National Academy of Sciences - PNAS 2004-06, Vol.101 (26), p.9648-9653
Hauptverfasser:	Rousseau, Erwann, Dehay, Benjamin, Ben-Haïem, Léa, Trottier, Yvon, Morange, Michel, Bertolotti, Anne, Jacob, François
Format:	Artikel
Sprache:	eng
Schlagworte:	Aggregation Antibodies Biological Sciences Cell aggregates Cell extracts Cell Line Cellular biology Cellular immunity Cytosol Endoplasmic Reticulum - metabolism Humans Huntingtin Protein Life Sciences Mitochondria Mitochondria - metabolism Mutation Nerve Tissue Proteins - chemistry Nerve Tissue Proteins - genetics Nerve Tissue Proteins - metabolism Neurons Nuclear Proteins - chemistry Nuclear Proteins - genetics Nuclear Proteins - metabolism Pathology Peptide Hydrolases - metabolism Peptides - chemistry Peptides - metabolism Prions Protease Inhibitors - pharmacology Proteasome Endopeptidase Complex Protein Denaturation - drug effects Protein Structure, Quaternary - drug effects Protein Transport Proteins Solubility
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