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Your search keyword '"Banaszynski LA"' showing total 3 results
Start Over Author "Banaszynski LA" Topic recombinant fusion proteins
3 results on '"Banaszynski LA"'

1. A general method for conditional regulation of protein stability in living animals.

Author

Sellmyer MA, Thorne SH, Banaszynski LA, Contag CH, and Wandless TJ

Subjects
Animals, Binding Sites genetics, Female, Gene Transfer Techniques, HCT116 Cells, Humans, Male, Mice, Morpholines metabolism, Neoplasm Transplantation, Neoplasms, Experimental genetics, Recombinant Fusion Proteins genetics, Tacrolimus Binding Proteins genetics, Transplantation, Heterologous, Neoplasms, Experimental metabolism, Protein Stability, Recombinant Fusion Proteins metabolism
Published
2009
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2. Regulating protein stability in mammalian cells using small molecules.

Author

Hagan EL, Banaszynski LA, Chen LC, Maynard-Smith LA, and Wandless TJ

Subjects
Animals, Binding Sites genetics, Cell Line, Humans, Ligands, Mice, Mutation, NIH 3T3 Cells, Plasmids genetics, Protein Binding, Recombinant Fusion Proteins genetics, Transfection, Protein Stability, Recombinant Fusion Proteins metabolism, Tacrolimus Binding Protein 1A genetics
Published
2009
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3. A rapid, reversible, and tunable method to regulate protein function in living cells using synthetic small molecules.

Author

Banaszynski LA, Chen LC, Maynard-Smith LA, Ooi AG, and Wandless TJ

Subjects
Animals, Ligands, Luminescent Proteins genetics, Mice, Mutation, NIH 3T3 Cells, Phenotype, Protein Binding, Protein Structure, Tertiary, Tacrolimus Binding Protein 1A chemistry, Tacrolimus Binding Proteins chemistry, Transfection, Gene Expression Regulation, Morpholines metabolism, Proteasome Endopeptidase Complex metabolism, Recombinant Fusion Proteins metabolism, Tacrolimus Binding Protein 1A genetics, Tacrolimus Binding Proteins genetics
Abstract

Rapid and reversible methods for perturbing the function of specific proteins are desirable tools for probing complex biological systems. We have developed a general technique to regulate the stability of specific proteins in mammalian cells using cell-permeable, synthetic molecules. We engineered mutants of the human FKBP12 protein that are rapidly and constitutively degraded when expressed in mammalian cells, and this instability is conferred to other proteins fused to these destabilizing domains. Addition of a synthetic ligand that binds to the destabilizing domains shields them from degradation, allowing fused proteins to perform their cellular functions. Genetic fusion of the destabilizing domain to a gene of interest ensures specificity, and the attendant small-molecule control confers speed, reversibility, and dose-dependence to this method. This general strategy for regulating protein stability should enable conditional perturbation of specific proteins with unprecedented control in a variety of experimental settings.

Published
2006
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