Evidence map›Paper›PMID 28468838›Full record

ArticleThe Biochemical journal2017

HIV-1 Tat potently stabilises Mdm2 and enhances viral replication.

Rameez Raja, Larance Ronsard, Sneh Lata, Shubhendu Trivedi, Akhil C Banerjea

Erratum issuedOpen access · hybridAbstract read
In one paragraph

Article in The Biochemical journal, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
1.7field-weighted citation impact, top 18% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

22 citing papers in PubMed, 27 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
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  8. Article
  9. Article
  10. CounterAKTing HIV: Toward a "Block and Clear" Strategy?Frontiers in cellular and infection microbiology · 2022
    Review
  11. Article
  12. Review
  13. Review
  14. Review
  15. Article
  16. Role of the Ubiquitin Proteasome System (UPS) in the HIV-1 Life Cycle.International journal of molecular sciences · 2019
    Review
  17. Article
  18. Article
  19. Article
  20. Scaling Synapses in the Presence of HIV.Neurochemical research · 2019
    Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors at 1 institution in 1 country.

Rameez RajaLaboratory of Virology, National Institute of Immunology, Aruna Asaf Ali Marg, New Delhi 110067, India akhil@nii.res.in akhil@nii.ac.in rameezraaj88@gmail.com rameez@nii.ac.in.
Larance Ronsard
Sneh LataLaboratory of Virology, National Institute of Immunology, Aruna Asaf Ali Marg, New Delhi 110067, India.
Shubhendu TrivediLaboratory of Virology, National Institute of Immunology, Aruna Asaf Ali Marg, New Delhi 110067, India.
Akhil C BanerjeaLaboratory of Virology, National Institute of Immunology, Aruna Asaf Ali Marg, New Delhi 110067, India akhil@nii.res.in akhil@nii.ac.in rameezraaj88@gmail.com rameez@nii.ac.in.
National Institute of Immunology · IN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Murine double minute 2 (Mdm2) is known to enhance the transactivation potential of human immunodeficiency virus (HIV-1) Tat protein by causing its ubiquitination. However, the regulation of Mdm2 during HIV-1 infection and its implications for viral replication have not been well studied. Here, we show that the Mdm2 protein level increases during HIV-1 infection and this effect is mediated by HIV-1 Tat protein. Tat appears to stabilise Mdm2 at the post-translational level by inducing its phosphorylation at serine-166 position through AKT. Although p53 is one of the key players for Mdm2 induction, Tat-mediated stabilisation of Mdm2 appears to be independent of p53. Moreover, the non-phosphorylatable mutant of Mdm2 (S166A) fails to interact with Tat and shows decreased half-life in the presence of Tat compared with wild-type Mdm2. Furthermore, the non-phosphorylatable mutant of Mdm2 (S166A) is unable to support HIV-1 replication. Thus, HIV-1 Tat appears to stabilise Mdm2, which in turn enhances Tat-mediated viral replication. This study highlights the importance of post-translational modifications of host cellular factors in HIV-1 replication and pathogenesis.

Indexed as

Cell Line, TumorCell NucleusGene Knockdown TechniquesHEK293 CellsHIV-1HumansMutationPhosphorylationProto-Oncogene Proteins c-mdm2RNA, Small Interferingtat Gene Products, Human Immunodeficiency VirusTumor Suppressor Protein p53Virus ReplicationProto-Oncogene Proteins c-mdm2RNA, Small Interferingtat Gene Products, Human Immunodeficiency VirusTP53 protein, humanTumor Suppressor Protein p53HIV-1 replicationMdm2phosphorylationTat

Identifiers

PMID28468838
PMCPMC5509382
OpenAlexW2611357885

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.