Title: | Tuning bulk electrostatics to regulate protein function |
Address: | "Department of Chemical and Systems Biology, Stanford University School of Medicine, MC 5174, Stanford, CA 94305, USA" |
DOI: | 10.1016/j.cell.2007.01.018 |
ISSN/ISBN: | 0092-8674 (Print) 0092-8674 (Linking) |
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" |
Keywords: | "Adaptor Proteins, Signal Transducing/chemistry/*metabolism Cyclin-Dependent Kinases/*metabolism Cyclins/*metabolism Pheromones/metabolism Phosphorylation Saccharomyces cerevisiae/cytology/*metabolism Saccharomyces cerevisiae Proteins/chemistry/*metabolism;" |
Notes: | "MedlineSerber, Zach Ferrell, James E Jr eng Comment 2007/02/10 Cell. 2007 Feb 9; 128(3):441-4. doi: 10.1016/j.cell.2007.01.018" |