Evidence map›Paper›PMID 27354282›Full record

ArticleThe Journal of biological chemistry2016

SLX4-SLX1 Protein-independent Down-regulation of MUS81-EME1 Protein by HIV-1 Viral Protein R (Vpr).

Xiaohong Zhou, Maria DeLucia, Jinwoo Ahn

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
3.4field-weighted citation impact, top 7% 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

31 citing papers in PubMed, 42 citations in OpenAlex.

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  20. HIV-1 Vpr counteracts HLTF-mediated restriction of HIV-1 infection in T cells.Proceedings of the National Academy of Sciences of the United States of America · 2019
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors at 1 institution in 1 country.

Xiaohong ZhouFrom the Department of Structural Biology and Pittsburgh Center for HIV Protein Interactions, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania 15260.
Maria DeLuciaFrom the Department of Structural Biology and Pittsburgh Center for HIV Protein Interactions, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania 15260.
Jinwoo AhnFrom the Department of Structural Biology and Pittsburgh Center for HIV Protein Interactions, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania 15260 jia12@pitt.edu.
University of Pittsburgh · US

Funding

X-Ray Core P50GM082251 · NIGMS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI CALERO, GUILLERMO ALBERTO · 2007 to 2018
$48.1M
Structure and function relationships regulating SAMHD1's dual enzymatic activitiesR01GM116642 · NIGMS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI AHN, JINWOO · 2015 to 2018
$1.4M
NIGMS NIH HHS P50 GM082251NIGMS NIH HHS R01 GM116642
6 · The paper itself

Abstract

Evolutionarily conserved structure-selective endonuclease MUS81 forms a complex with EME1 and further associates with another endonuclease SLX4-SLX1 to form a four-subunit complex of MUS81-EME1-SLX4-SLX1, coordinating distinctive biochemical activities of both endonucleases in DNA repair. Viral protein R (Vpr), a highly conserved accessory protein in primate lentiviruses, was previously reported to bind SLX4 to mediate down-regulation of MUS81. However, the detailed mechanism underlying MUS81 down-regulation is unclear. Here, we report that HIV-1 Vpr down-regulates both MUS81 and its cofactor EME1 by hijacking the host CRL4-DCAF1 E3 ubiquitin ligase. Multiple Vpr variants, from HIV-1 and SIV, down-regulate both MUS81 and EME1. Furthermore, a C-terminally truncated Vpr mutant and point mutants R80A and Q65R, all of which lack G2 arrest activity, are able to down-regulate MUS81-EME1, suggesting that Vpr-induced G2 arrest is not correlated with MUS81-EME1 down-regulation. We also show that neither the interaction of MUS81-EME1 with Vpr nor their down-regulation is dependent on SLX4-SLX1. Together, these data provide new insight on a conserved function of Vpr in a host endonuclease down-regulation.

Indexed as

Down-RegulationAmino Acid SubstitutionCarrier ProteinsCell LineDNA-Binding ProteinsEndodeoxyribonucleasesEndonucleasesHIV-1HumansMutation, MissenseProtein Serine-Threonine KinasesReceptors, Interleukin-17RecombinasesUbiquitin-Protein Ligasesvpr Gene Products, Human Immunodeficiency VirusCarrier ProteinsDCAF1 protein, humanDNA-Binding ProteinsEme1 protein, humanEndodeoxyribonucleasesEndonucleasesIL17RB protein, humanMUS81 protein, humanProtein Serine-Threonine KinasesReceptors, Interleukin-17RecombinasesSLX1 protein, humanSLX4 protein, humanUbiquitin-Protein Ligasesvpr Gene Products, Human Immunodeficiency Virusvpr protein, Human immunodeficiency virus 1E3 ubiquitin ligasehuman immunodeficiency virus (HIV)proteasomeprotein degradationviral proteinWestern blot

Identifiers

PMID27354282
PMCPMC5016100
OpenAlexW2465217654

What OpenQuestion holds

Textmetadata
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.