title: Recent progress with FKBP-derived destabilizing domains.
abstract: The FKBP-derived destabilizing domains are increasingly being used to confer small molecule-dependent stability to many different proteins. The L106P domain confers instability to yellow fluorescent protein when it is fused to the N-terminus, the C-terminus, or spliced into the middle of yellow fluorescent protein, however multiple copies of L106P do not confer greater instability. These engineered destabilizing domains are not dominant to endogenous degrons that regulate protein stability.
authors.affiliation: Department of Chemical and Systems Biology, Stanford University, 318 Campus Drive, Clark Center W350A, Stanford, CA 94305-5441, USA.
authors.forename: Bernard W
authors.initials: BW
authors.lastname: Chu
authors.forename: Laura A
authors.initials: LA
authors.lastname: Banaszynski
authors.forename: Ling-chun
authors.initials: LC
authors.lastname: Chen
authors.forename: Thomas J
authors.initials: TJ
authors.lastname: Wandless
mesh_terms: D020816:Amino Acid Motifs; D002453:Cell Cycle / Q000187:drug effects; D019926:Cyclin B / Q000378:metabolism; D056744:Cyclin B1; D006367:HeLa Cells; D006801:Humans; D008958:Models, Molecular; D013329:Structure-Activity Relationship; D022021:Tacrolimus Binding Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism
chemical_list: C534699:CCNB1 protein, human; D019926:Cyclin B; D056744:Cyclin B1; D022021:Tacrolimus Binding Proteins