title: Fluorescence fluctuation spectroscopy and imaging methods for examination of dynamic protein interactions in yeast.
abstract: Protein interactions are inherently dynamic. In no system is this more true and important than in signaling pathways, where spatial and temporal control of specific protein interactions is key to signaling specificity and timing. While genetic and biochemical interactions form a necessary and important starting point for deciphering interactions among signaling components, they struggle to provide precise information of where and when interactions occur in a live cell setting. In contrast, live cell fluorescence studies such as those outlined below are able to provide quantitative information on the strength, nature, timing, and location of homotypic and heterotypic protein interactions.
authors.affiliation: Stowers Institute for Medical Research, Kansas City, MO, USA. brs@stowers.org
authors.forename: Brian D
authors.initials: BD
authors.lastname: Slaughter
authors.forename: Jay R
authors.initials: JR
authors.lastname: Unruh
authors.forename: Rong
authors.initials: R
authors.lastname: Li
mesh_terms: D002462:Cell Membrane / Q000378:metabolism; D002470:Cell Survival; D003116:Color; D046508:Culture Techniques; D031541:Fluorescence Resonance Energy Transfer / Q000379:methods*; D005656:Fungal Proteins / Q000302:isolation & purification / Q000378:metabolism*; D057054:Molecular Imaging / Q000379:methods*; D038761:Photobleaching; D017785:Photons; D025941:Protein Interaction Mapping / Q000379:methods*; D012441:Saccharomyces cerevisiae / Q000166:cytology / Q000254:growth & development / Q000378:metabolism*
chemical_list: D005656:Fungal Proteins