Co-chaperone CHIP promotes aggregation of ataxin-1

Recent studies demonstrated that co-chaperone/E3 ligase CHIP (C-terminus of hsp70-interacting protein) mediates the ubiquitylation and suppresses the aggregation of polyglutamine (polyQ) proteins, such as huntingtin or ataxin-3. In this study, we investigated the effects of CHIP on the degradation o...

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Veröffentlicht in:	Molecular and cellular neuroscience 2007, Vol.34 (1), p.69-79
Hauptverfasser:	Choi, Jung Young, Ryu, Jeong Hee, Kim, Hyo-Sun, Park, Sung Goo, Bae, Kwang-Hee, Kang, Sunghyun, Myung, Pyung Keun, Cho, Sayeon, Park, Byoung Chul, Lee, Do Hee
Format:	Artikel
Sprache:	eng
Schlagworte:	Aggregation Amino Acid Sequence - genetics Ataxin-1 Ataxins Cell Line CHIP Heredodegenerative Disorders, Nervous System - genetics Heredodegenerative Disorders, Nervous System - metabolism Heredodegenerative Disorders, Nervous System - physiopathology Humans Inclusion Bodies - genetics Inclusion Bodies - metabolism Molecular Chaperones - genetics Molecular Chaperones - metabolism Nerve Degeneration - genetics Nerve Degeneration - metabolism Nerve Tissue Proteins - genetics Nerve Tissue Proteins - metabolism Neurodegeneration Nuclear Proteins - genetics Nuclear Proteins - metabolism Peptides - metabolism Point Mutation - genetics Polyglutamine Protein Structure, Tertiary - genetics Trinucleotide Repeat Expansion - genetics Ubiquitin Ubiquitin - metabolism Ubiquitin-Protein Ligases - chemistry Ubiquitin-Protein Ligases - genetics Ubiquitin-Protein Ligases - metabolism
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