PUBLICATION
Nanobody-targeted E3-ubiquitin ligase complex degrades nuclear proteins
- Authors
- Ju Shin, Y., Kyun Park, S., Jung Jung, Y., Na Kim, Y., Sung Kim, K., Kyu Park, O., Kwon, S.H., Ho Jeon, S., Trinh, l.e. .A., Fraser, S.E., Kee, Y., Joon Hwang, B.
- ID
- ZDB-PUB-150917-10
- Date
- 2015
- Source
- Scientific Reports 5: 14269 (Journal)
- Registered Authors
- Fraser, Scott E., Trinh, Le
- Keywords
- none
- MeSH Terms
-
- Animals
- Gene Expression
- Genes, Reporter
- HMGA2 Protein/genetics
- HMGA2 Protein/metabolism
- Nuclear Proteins/genetics
- Nuclear Proteins/metabolism*
- Protein Binding
- Proteolysis
- RNA Interference
- Recombinant Fusion Proteins/genetics
- Recombinant Fusion Proteins/metabolism
- Single-Domain Antibodies/immunology
- Single-Domain Antibodies/metabolism*
- Ubiquitin-Protein Ligase Complexes/immunology
- Ubiquitin-Protein Ligase Complexes/metabolism*
- Ubiquitin-Protein Ligases/genetics
- Ubiquitin-Protein Ligases/immunology
- Ubiquitin-Protein Ligases/metabolism*
- Ubiquitination
- Zebrafish
- PubMed
- 26373678 Full text @ Sci. Rep.
Citation
Ju Shin, Y., Kyun Park, S., Jung Jung, Y., Na Kim, Y., Sung Kim, K., Kyu Park, O., Kwon, S.H., Ho Jeon, S., Trinh, l.e. .A., Fraser, S.E., Kee, Y., Joon Hwang, B. (2015) Nanobody-targeted E3-ubiquitin ligase complex degrades nuclear proteins. Scientific Reports. 5:14269.
Abstract
Targeted protein degradation is a powerful tool in determining the function of specific proteins or protein complexes. We fused nanobodies to SPOP, an adaptor protein of the Cullin-RING E3 ubiquitin ligase complex, resulting in rapid ubiquitination and subsequent proteasome-dependent degradation of specific nuclear proteins in mammalian cells and zebrafish embryos. This approach is easily modifiable, as substrate specificity is conferred by an antibody domain that can be adapted to target virtually any protein.
Genes / Markers
Expression
Phenotype
Mutations / Transgenics
Human Disease / Model
Sequence Targeting Reagents
Fish
Orthology
Engineered Foreign Genes
Mapping