title: Tuning bulk electrostatics to regulate protein function.
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.
authors.affiliation: Department of Chemical and Systems Biology, Stanford University School of Medicine, MC 5174, Stanford, CA 94305, USA.
authors.forename: Zach
authors.initials: Z
authors.lastname: Serber
authors.forename: James E
authors.initials: JE
authors.lastname: Ferrell
mesh_terms: D048868:Adaptor Proteins, Signal Transducing / Q000737:chemistry / Q000378:metabolism*; D018844:Cyclin-Dependent Kinases / Q000378:metabolism*; D016213:Cyclins / Q000378:metabolism*; D010675:Pheromones / Q000378:metabolism; D010766:Phosphorylation; D012441:Saccharomyces cerevisiae / Q000166:cytology / Q000378:metabolism*; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry / Q000378:metabolism*; D055672:Static Electricity
chemical_list: D048868:Adaptor Proteins, Signal Transducing; D016213:Cyclins; D010675:Pheromones; C080321:STE5 protein, S cerevisiae; D029701:Saccharomyces cerevisiae Proteins; D018844:Cyclin-Dependent Kinases