Transcription factor sequestration by polyglutamine proteins.
In polyglutamine diseases including Huntington's disease, the causative gene products containing expanded polyglutamine form nuclear aggregates in neurons. Recent studies have identified several transcriptional factors, which interact with and are sequestered by expanded polyglutamine aggregates in neurons. Further, altered expression of many genes has been shown in several polyglutamine disease models. These observations suggest an involvement of transcriptional dysregulation in pathological process of these diseases. In this chapter, we introduce several methods to examine the interaction of transcriptional factors with and their sequestration by expanded polyglutamine proteins in vitro and in vivo.
Yamanaka
Tomoyuki
T
Nukina
Nobuyuki
N
D000818:Animals; D001671:Biochemistry / Q000379:methods*; D001681:Biological Assay; D015153:Blotting, Western; D002478:Cells, Cultured; D004195:Disease Models, Animal; D024202:Electrophoretic Mobility Shift Assay; D005455:Fluorescent Antibody Technique; D006801:Humans; D006816:Huntington Disease / Q000378:metabolism; D051379:Mice; D050505:Mutant Proteins / Q000737:chemistry / Q000378:metabolism; D009419:Nerve Tissue Proteins / Q000737:chemistry / Q000378:metabolism*; D010455:Peptides / Q000378:metabolism*; D011485:Protein Binding; D020836:Protein Structure, Quaternary; D014020:Tissue Extracts; D014157:Transcription Factors / Q000378:metabolism*; D014162:Transfection
D050505:Mutant Proteins; D009419:Nerve Tissue Proteins; D010455:Peptides; D014020:Tissue Extracts; D014157:Transcription Factors; C097188:polyglutamine