Tuning bulk electrostatics to regulate protein function

Cell. 2007 Feb 9;128(3):441-4. doi: 10.1016/j.cell.2007.01.018.

Abstract

Cyclin-dependent kinase activation can prevent yeast cells from responding to mating pheromone. Strickfaden et al. (2007) now show that this block arises from the multisite phosphorylation of Ste5. This provides a beautiful example of how phosphorylation can produce decisive changes in protein function through bulk electrostatics, without the necessity of intricate conformational changes.

Publication types

  • Comment

MeSH terms

  • Adaptor Proteins, Signal Transducing / chemistry
  • Adaptor Proteins, Signal Transducing / metabolism*
  • Cyclin-Dependent Kinases / metabolism*
  • Cyclins / metabolism*
  • Pheromones / metabolism
  • Phosphorylation
  • Saccharomyces cerevisiae / cytology
  • Saccharomyces cerevisiae / metabolism*
  • Saccharomyces cerevisiae Proteins / chemistry
  • Saccharomyces cerevisiae Proteins / metabolism*
  • Static Electricity

Substances

  • Adaptor Proteins, Signal Transducing
  • Cyclins
  • Pheromones
  • STE5 protein, S cerevisiae
  • Saccharomyces cerevisiae Proteins
  • Cyclin-Dependent Kinases