ZFIN ID: ZDB-PUB-150917-10
Nanobody-targeted E3-ubiquitin ligase complex degrades nuclear proteins
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.
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.
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.