4.6 Review

Prions, protein homeostasis, and phenotypic diversity

Journal

TRENDS IN CELL BIOLOGY
Volume 20, Issue 3, Pages 125-133

Publisher

ELSEVIER SCIENCE LONDON
DOI: 10.1016/j.tcb.2009.12.003

Keywords

-

Categories

Funding

  1. National Science Foundation (NSF)
  2. Deutsche Forschungsgemeinschaft (DFG)
  3. G. Harold & Leila Y. Mathers Foundation
  4. NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM025874] Funding Source: NIH RePORTER

Ask authors/readers for more resources

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.

Authors

I am an author on this paper
Click your name to claim this paper and add it to your profile.

Reviews

Primary Rating

4.6
Not enough ratings

Secondary Ratings

Novelty
-
Significance
-
Scientific rigor
-
Rate this paper

Recommended

No Data Available
No Data Available