ArticleBiochemistry and biophysics reports2022
A siRNA screening of UBE2 family demonstrated that UBE2R1 had a high repressive effect on HIV Tat protein.
Article in Biochemistry and biophysics reports, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
2 citing papers in PubMed, 4 citations in OpenAlex.
- TRIP12 promotes HIV-1 replication and latency reactivation by stabilizing Tat via USP7-mediated deubiquitination.Journal of virology · 2026Article
- Compensatory reactions of B cells in response to chronic HIV-1 Tat exposure.Journal of cellular physiology · 2025Article
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Authors and funding
2 authors at 2 institutions in 2 countries.
Funding
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Abstract
HIV Tat is an essential protein required for the transcription elongation of HIV genome. It has been shown that Tat can be degraded by either proteasome or autophagy pathways. In this study, it was shown that proteasome inhibitor MG132 could significantly prevent HIV Tat protein degradation in Tat over-expressing HeLa cells but it had a moderate effect in preventing Tat protein degradation in Jurkat T cells. A screening of the available UBE2 siRNA family identified that UBE2R1 had a high repressive effect on Tat protein but not on Tat mRNA level. This study further showed that RNF20 might not be the E3 ligase of Tat but was required to maintain a high level of H2B-monoubiquitylation (H2Bub1) on HIV-1 genome for efficient elongation. Overall, our study indicated that UBE2R1 might be the potential ubiquitin E2 ligase for HIV Tat protein turnover and RNF20 regulated HIV expression in the transcription elongation level.
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