Related Experiment Video
Updated: Aug 16, 2026

Fractionation for Resolution of Soluble and Insoluble Huntingtin Species
Published on: February 27, 2018
BAG-1 associates with the polyglutamine-expanded huntingtin aggregates
Nihar Ranjan Jana1, Nobuyuki Nukina
1Cellular and Molecular Neuroscience Laboratory, National Brain Research Centre, Manesar, Gurgaon 122050, India. nihar@nbrc.ac.in
Abstract:
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.
More Related Videos
Related Concept Videos
Amyloid Fibrils
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining, normally used to...
Ligand Binding and Linkage
Huntington Disease l: Introduction

