Chaperones in neurodegeneration

Iris Lindberg, James Shorter, R. Luke Wiseman, Fabrizio Chiti, Chad A. Dickey, Pamela J. McLean

Research output: Contribution to journalReview articlepeer-review

44 Scopus citations

Abstract

Cellular protein homeostasis (proteostasis) maintains the integrity of the proteome and includes protein synthesis, folding, oligomerization, and turnover; chaperone proteins assist with all of these processes. Neurons appear to be especially susceptible to failures in proteostasis, and this is now increasingly recognized as a major origin of neurodegenerative disease. This review, based on a minisymposium presented at the 2015 Society for Neuroscience meeting, describes new work in the area of neuronal proteostasis, with a specific focus on the roles and therapeutic uses of protein chaperones. We first present a brief review of protein misfolding and aggregation in neurodegenerative disease. We then discuss different aspects of chaperone control of neuronal proteostasis on topics ranging from chaperone engineering, to chaperone-mediated blockade of protein oligomerization and cytotoxicity, to the potential rescue of neurodegenerative processes using modified chaperone proteins.

Original languageEnglish (US)
Pages (from-to)13853-13859
Number of pages7
JournalJournal of Neuroscience
Volume35
Issue number41
DOIs
StatePublished - Oct 14 2015

Keywords

  • Chaperone
  • Heat shock proteins
  • Neurodegeneration
  • Parkinson’s disease
  • Protein misfolding
  • Proteostasis

ASJC Scopus subject areas

  • Neuroscience(all)

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