Generation of conditional auxin-inducible degron (AID) cells and tight control of degron-fused proteins using the degradation inhibitor auxinole

Methods. 2019 Jul 15:164-165:73-80. doi: 10.1016/j.ymeth.2019.04.010. Epub 2019 Apr 24.

Abstract

Controlling protein expression using a degron is advantageous because the protein of interest can be rapidly depleted in a reversible manner. We pioneered the development of the auxin-inducible degron (AID) technology by transplanting a plant-specific degradation pathway to non-plant cells. In human cells expressing an E3 ligase component, OsTIR1, it is possible to degrade a degron-fused protein with a half-life of 15-45 min in the presence of the phytohormone auxin. We reported previously the generation of human HCT116 mutants in which the C terminus of endogenous proteins was fused with the degron by CRISPR-Cas9-based knock-in. Here, we show new plasmids for N-terminal tagging and describe a detailed protocol for the generation of AID mutants of human HCT116 and DLD1 cells. Moreover, we report the use of an OsTIR1 inhibitor, auxinole, to suppress leaky degradation of degron-fused proteins. The addition of auxinole is also useful for rapid re-expression after depletion of degron-fused proteins. These improvements enhance the utility of AID technology for studying protein function in living human cells.

Keywords: Auxin; Conditional mutant; Degradation inhibitor; Degron; Genome editing; Protein degradation.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • CRISPR-Cas Systems / genetics
  • Cell Culture Techniques / methods
  • Genetic Vectors / genetics
  • HCT116 Cells
  • Half-Life
  • Humans
  • Indoleacetic Acids / pharmacology*
  • Luminescent Proteins / genetics
  • Luminescent Proteins / metabolism
  • Plant Proteins / antagonists & inhibitors
  • Plant Proteins / genetics
  • Plant Proteins / metabolism
  • Plasmids / genetics
  • Proteolysis / drug effects*
  • Recombinant Fusion Proteins / genetics
  • Recombinant Fusion Proteins / metabolism*
  • Transfection / methods
  • Ubiquitin-Protein Ligases / antagonists & inhibitors
  • Ubiquitin-Protein Ligases / genetics
  • Ubiquitin-Protein Ligases / metabolism

Substances

  • Indoleacetic Acids
  • Luminescent Proteins
  • Plant Proteins
  • Recombinant Fusion Proteins
  • alpha-(2,4-dimethylphenylethyl-2-oxo)indole-3-acetic acid
  • Ubiquitin-Protein Ligases