BAG-1 associates with the polyglutamine-expanded huntingtin aggregates.
Huntington's disease (HD) is characterised by the proteolytic production of N-terminal fragments of huntingtin containing polyglutamine repeats that forms intracellular ubiquitinated aggregates in the affected neurons. Using cellular and transgenic mice model of HD, we report here that BAG-1 co-immunoprecipitates with the polyglutamine-expanded truncated N-terminal huntingtin (tNhtt) and associates with ... their aggregates through its interaction with the chaperones Hsc70/Hsp70. We further demonstrate that the over expression of BAG-1 protects polyglutamine-expanded tNhtt induced cell death. Since, BAG-1 is essential for cell survival, its association with tNhtt aggregates might disrupt its normal function and thereby promote polyglutamine-expanded tNhtt-induced cell death.
Mesh Terms:
Animals, Brain, Carrier Proteins, Cell Death, Cell Line, Cell Survival, DNA-Binding Proteins, Disease Models, Animal, HSC70 Heat-Shock Proteins, HSP70 Heat-Shock Proteins, Huntington Disease, Inclusion Bodies, Macromolecular Substances, Mice, Mice, Transgenic, Nerve Degeneration, Nerve Tissue Proteins, Nuclear Proteins, Peptide Fragments, Peptides, Transcription Factors, Trinucleotide Repeat Expansion
Animals, Brain, Carrier Proteins, Cell Death, Cell Line, Cell Survival, DNA-Binding Proteins, Disease Models, Animal, HSC70 Heat-Shock Proteins, HSP70 Heat-Shock Proteins, Huntington Disease, Inclusion Bodies, Macromolecular Substances, Mice, Mice, Transgenic, Nerve Degeneration, Nerve Tissue Proteins, Nuclear Proteins, Peptide Fragments, Peptides, Transcription Factors, Trinucleotide Repeat Expansion
Neurosci. Lett.
Date: Apr. 22, 2005
PubMed ID: 15781153
View in: Pubmed Google Scholar
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