Caenorhabditis elegans as a model system for studying non-cellautonomous mechanisms in protein-misfolding diseases

Carmen I. Nussbaum-Krammer, Richard I. Morimoto*

*Corresponding author for this work

Research output: Contribution to journalReview articlepeer-review

45 Scopus citations


Caenorhabditis elegans has a number of distinct advantages that are useful for understanding the basis for cellular and organismal dysfunction underlying age-associated diseases of protein misfolding. Although protein aggregation, a key feature of human neurodegenerative diseases, has been typically explored in vivo at the single-cell level using cells in culture, there is now increasing evidence that proteotoxicity has a non-cell-autonomous component and is communicated between cells and tissues in a multicellular organism. These discoveries have opened up new avenues for the use of C. elegans as an ideal animal model system to study non-cellautonomous proteotoxicity, prion-like propagation of aggregationprone proteins, and the organismal regulation of stress responses and proteostasis. This Review focuses on recent evidence that C. elegans has mechanisms to transmit certain classes of toxic proteins between tissues and a complex stress response that integrates and coordinates signals from single cells and tissues across the organism. These findings emphasize the potential of C. elegans to provide insights into non-cell-autonomous proteotoxic mechanisms underlying age-related protein-misfolding diseases.

Original languageEnglish (US)
Pages (from-to)31-39
Number of pages9
JournalDMM Disease Models and Mechanisms
Issue number1
StatePublished - Jan 2014


  • Caenorhabditis elegans
  • Cell non-autonomous proteotoxicity
  • Prion-like spreading

ASJC Scopus subject areas

  • Neuroscience (miscellaneous)
  • Medicine (miscellaneous)
  • Immunology and Microbiology (miscellaneous)
  • Biochemistry, Genetics and Molecular Biology(all)


Dive into the research topics of 'Caenorhabditis elegans as a model system for studying non-cellautonomous mechanisms in protein-misfolding diseases'. Together they form a unique fingerprint.

Cite this