Huntington's Disease Research Today is a free monthly online journal that collates and summarizes the latest research about Huntington's Disease, including details on genetics, causes, symptoms, treatment.

BAG-1 associates with the polyglutamine-expanded huntingtin aggregates.

Jana NR, Nukina N

Cellular and Molecular Neuroscience Laboratory, National Brain Research Centre, Manesar, Gurgaon 122050, India. nihar@nbrc.ac.in

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.

Published 22 March 2005 in Neurosci Lett, 378(3): 171-5.
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