Prions, protein homeostasis, and phenotypic diversity

Research output: Contribution to journalResearch articleContributedpeer-review

Contributors

  • Randal Halfmann - , Whitehead Institute for Biomedical Research, Massachusetts Institute of Technology (MIT) (Author)
  • Simon Alberti - , Whitehead Institute for Biomedical Research (Author)
  • Susan Lindquist - , Whitehead Institute for Biomedical Research, Howard Hughes Medical Institute, Massachusetts Institute of Technology (MIT) (Author)

Abstract

Prions are fascinating but often misunderstood protein aggregation phenomena. The traditional association of the mammalian prion protein with disease has overshadowed a potentially more interesting attribute of prions: their ability to create protein-based molecular memories. In fungi, prions alter the relationship between genotype and phenotype in a heritable way that diversifies clonal populations. Recent findings in yeast indicate that prions might be much more common than previously realized. Moreover, prion-driven phenotypic diversity increases under stress, and can be amplified by the dynamic maturation of prion-initiating states. In this article, we suggest that these qualities allow prions to act as 'bet-hedging' devices that facilitate the adaptation of yeasts to stressful environments, and might speed the evolution of new traits.

Details

Original languageEnglish
Pages (from-to)125-133
Number of pages9
JournalTrends in cell biology
Volume20
Issue number3
Publication statusPublished - Mar 2010
Peer-reviewedYes
Externally publishedYes

External IDs

PubMed 20071174
ORCID /0000-0003-4017-6505/work/161409872

Keywords

ASJC Scopus subject areas