Evidence map›Paper›PMID 31797533›Full record

ArticleEMBO reports2020

TRIM21-mediated proteasomal degradation of SAMHD1 regulates its antiviral activity.

Zhaolong Li, Chen Huan, Hong Wang, Yue Liu, Xin Liu, Xing Su, Jinghua Yu, Zhilei Zhao, Xiao-Fang Yu, Baisong Zheng and 1 more

Open access · hybridAbstract read
In one paragraph

Article in EMBO reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed
2.6field-weighted citation impact, top 9% 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

46 citing papers in PubMed, 74 citations in OpenAlex.

  1. Article
  2. TRIM21 is a molecular rheostat for influenza A virus replication.bioRxiv : the preprint server for biology · 2026
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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

11 authors at 1 institution in 1 country.

Zhaolong LiThe First Hospital of Jilin University, Institute of Virology and AIDS Research, Changchun, China.
Chen HuanThe First Hospital of Jilin University, Institute of Virology and AIDS Research, Changchun, China.
Hong WangThe First Hospital of Jilin University, Institute of Virology and AIDS Research, Changchun, China.
Yue LiuThe First Hospital of Jilin University, Institute of Virology and AIDS Research, Changchun, China.
Xin LiuThe First Hospital of Jilin University, Institute of Virology and AIDS Research, Changchun, China.
Xing SuThe First Hospital of Jilin University, Institute of Virology and AIDS Research, Changchun, China.
Jinghua YuThe First Hospital of Jilin University, Institute of Virology and AIDS Research, Changchun, China.
Zhilei ZhaoThe First Hospital of Jilin University, Institute of Virology and AIDS Research, Changchun, China.
Xiao-Fang YuThe First Hospital of Jilin University, Institute of Virology and AIDS Research, Changchun, China.
Baisong ZhengThe First Hospital of Jilin University, Institute of Virology and AIDS Research, Changchun, China.
Wenyan ZhangThe First Hospital of Jilin University, Institute of Virology and AIDS Research, Changchun, China.ORCID 0000-0003-4507-521X
Jilin University · CN

Funding

Chinese Ministry of Science and Technology 2018ZX10302104-001-010Graduate Innovation Fund of Jilin UniversityJLU | Program for Jilin University Science and Technology Innovative Research Team (Program for JLU Science and Technology Innovative Research Team) JLUSTIRT, 2017TD-05Key Laboratory of Molecular Virology, Jilin Province 20102209NSF | Foundation for Innovative Research Groups of the National Natural Science Foundation of China 31270202NSF | Foundation for Innovative Research Groups of the National Natural Science Foundation of China 81672004NSF | Foundation for Innovative Research Groups of the National Natural Science Foundation of China 81701987Science and Technology Department of Jilin Province 20190101003JHYouth Foundation of the First Hospital of Jilin University JDYY82017003
6 · The paper itself

Abstract

SAMHD1 possesses multiple functions, but whether cellular factors regulate SAMHD1 expression or its function remains not well characterized. Here, by investigating why cultured RD and HEK293T cells show different sensitivity to enterovirus 71 (EV71) infection, we demonstrate that SAMHD1 is a restriction factor for EV71. Importantly, we identify TRIM21, an E3 ubiquitin ligase, as a key regulator of SAMHD1, which specifically interacts and degrades SAMHD1 through the proteasomal pathway. However, TRIM21 has no effect on EV71 replication itself. Moreover, we prove that interferon production stimulated by EV71 infection induces increased TRIM21 and SAMHD1 expression, whereas increasing TRIM21 overrides SAMHD1 inhibition of EV71 in cells and in a neonatal mouse model. TRIM21-mediated degradation of SAMHD1 also affects SAMHD1-dependent restriction of HIV-1 and the regulation of interferon production. We further identify the functional domains in TRIM21 required for SAMHD1 binding and the ubiquitination site K622 in SAMHD1 and show that phosphorylation of SAMHD1 at T592 also blocks EV71 restriction. Our findings illuminate how EV71 overcomes SAMHD1 inhibition via the upregulation of TRIM21.

Indexed as

Antiviral AgentsHIV-1AnimalsHEK293 CellsHumansMiceSAM Domain and HD Domain-Containing Protein 1UbiquitinationAntiviral AgentsSAM Domain and HD Domain-Containing Protein 1SAMHD1 protein, humanEV71 infectioninterferon inductionregulationSAMHD1 inhibitionubiquitin-proteasome degradation

Identifiers

PMID31797533
PMCPMC6944907
OpenAlexW2992149043

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.