Brain CHIP: removing the culprits in neurodegenerative disease

Chad A. Dickey, Cam Patterson, Dennis Dickson, Leonard Petrucelli

Research output: Contribution to journalReview article

74 Scopus citations

Abstract

A factor that is common to the most-frequent neurodegenerative diseases is the accumulation of abnormal proteins that are associated with cellular dysfunction. Contrary to years of speculation, recent evidence suggests that soluble intermediates - not the visible pathological aggregates associated with disease - are the cause of neurotoxicity. These findings suggest that aggregate formation might be an adaptive stress response that is facilitated by neuronal protein triage molecules. In particular, the molecular co-chaperone CHIP (C terminus of HSC70-interacting protein) has been linked to several of these disorders, serving as a crucial catalyst for the ubiquitination of several heat shock protein (HSP)70 client proteins that are involved in neurodegenerative disease. Therefore, understanding the mechanisms that are involved in CHIP-mediated protein trafficking might provide invaluable clues to neuronal function, both in normal and diseased conditions.

Original languageEnglish (US)
Pages (from-to)32-38
Number of pages7
JournalTrends in Molecular Medicine
Volume13
Issue number1
DOIs
StatePublished - Jan 1 2007

ASJC Scopus subject areas

  • Molecular Medicine
  • Molecular Biology

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