ArticleProtein science : a publication of the Protein Society2018
Unique auto-ubiquitination activities of artificial RING fingers in cancer cells.
Article in Protein science : a publication of the Protein Society, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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Who cites it
3 citing papers in PubMed, 6 citations in OpenAlex.
- Solution structure of the zinc finger domain of human RNF144A ubiquitin ligase.Protein science : a publication of the Protein Society · 2020Article
- Zinc finger domain of the human DTX protein adopts a unique RING fold.Protein science : a publication of the Protein Society · 2019Article
- Unique RING finger structure from the human HRD1 protein.Protein science : a publication of the Protein Society · 2019Article
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Authors and funding
4 authors at 1 institution in 1 country.
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Abstract
Ubiquitin-conjugating (E2) enzymes in protein ubiquitination are associated with various diseases. An artificial RING finger (ARF) is a useful tool, and E2 activities are conveniently estimated based on ARF reactivities. To extend the use of ARF in cells, we constructed a TAT-ARF using a cell-penetrating trans-activator protein (TAT) peptide. An in vitro ubiquitination assay without substrates showed auto-ubiquitination of TAT-ARF via its TAT region. TAT-ARF was translocated into MCF7 breast cancer cells, and then TAT-ARF ubiquitinated itself via its ARF. Experiments using confocal laser-scanning microscopy revealed that FAM-labeled TAT-ARF was readily internalized in cells and it remained encapsulated in vesicles. The Cell Counting Kit-8 assay indicated that the TAT-ARF uptake occurred without cytotoxicity in MCF7 cells at concentrations below 5.0 μM. By taking advantage of TAT-ARF, we, for the first time, succeeded in detecting E2 activities in cells. Thus, the present work opens up new avenues in the investigation of protein ubiquitination.
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