Polyglutamine aggregates alter protein folding homeostasis in Caenorhabditis elegans

• DOI: 10.1073/pnas.100107297
• Publication Date: 2002-07-26T14:35:07Z
• Authors: Sanjeev H. Satyal; Enrico Schmidt; Kazunori Kitagawa; Neal Sondheimer; Susan Lindquist; James M. Kramer; Richard I. Morimoto
• Keywords: Chaperone (clinical)

Expansion of polyglutamine repeats in several unrelated proteins causes neurodegenerative diseases with distinct but related pathologies. To provide a model system for investigating common pathogenic features, we have examined the behavior expansions expressed Caenorhabditis elegans . The expression as green fluorescent protein (GFP)-fusion body wall muscle cells discrete cytoplasmic aggregates that appear early embryogenesis and correlates delay larval to adult development. heat shock response is activated idiosyncratically individual length-dependent fashion. toxic effect formation can be reversed by coexpression yeast chaperone Hsp104. altered homeostasis associated both sequestration an otherwise soluble shorter arrays glutamine relocalization nuclear glutamine-rich protein. These observations induced aggregation implications disorders involving aggregation.