Evidence map›Paper›PMID 40641422›Full record

ArticleAdvanced science (Weinheim, Baden-Wurttemberg, Germany)2025

API5 Phosphorylation Promotes Antiviral Immunity by Inhibiting Degradation of Cytosolic RNA Sensor RLRs.

Tingjuan Deng, Jianan Xu, Linglong Qin, Xingbo Wang, Chenhe Lu, Yanming Huang, Da Liu, Yan Yan, Weiren Dong, Pinglong Xu and 1 more

Abstract read
In one paragraph

Article in Advanced science (Weinheim, Baden-Wurttemberg, Germany), 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–field-weighted citation impact
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

2 citing papers in PubMed.

  1. Article
  2. Article
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.

Tingjuan DengMOA Key Laboratory of Animal Virology, Zhejiang University Center for Veterinary Sciences, Hangzhou, 310058, China.
Jianan XuMOA Key Laboratory of Animal Virology, Zhejiang University Center for Veterinary Sciences, Hangzhou, 310058, China.
Linglong QinMOA Key Laboratory of Animal Virology, Zhejiang University Center for Veterinary Sciences, Hangzhou, 310058, China.
Xingbo WangMOA Key Laboratory of Animal Virology, Zhejiang University Center for Veterinary Sciences, Hangzhou, 310058, China.
Chenhe LuMOA Key Laboratory of Animal Virology, Zhejiang University Center for Veterinary Sciences, Hangzhou, 310058, China.
Yanming HuangMOA Key Laboratory of Animal Virology, Zhejiang University Center for Veterinary Sciences, Hangzhou, 310058, China.
Da LiuMOA Key Laboratory of Animal Virology, Zhejiang University Center for Veterinary Sciences, Hangzhou, 310058, China.
Yan YanMOA Key Laboratory of Animal Virology, Zhejiang University Center for Veterinary Sciences, Hangzhou, 310058, China.
Weiren DongMOA Key Laboratory of Animal Virology, Zhejiang University Center for Veterinary Sciences, Hangzhou, 310058, China.
Pinglong XuState Key Laboratory for Diagnosis and Treatment of Severe Infectious Diseases, First Affiliated Hospital, Zhejiang University, Hangzhou, 310058, China.
Jiyong ZhouMOA Key Laboratory of Animal Virology, Zhejiang University Center for Veterinary Sciences, Hangzhou, 310058, China.ORCID https://orcid.org/0000-0002-8852-1227

Funding

Fundamental Research Funds for the Central Universities 2022-KYY-517101-0005National Natural Science Foundation of China 32192454National Natural Science Foundation of China 32302847
6 · The paper itself

Abstract

Ubiquitin-mediated selective autophagy is essential for innate immune responses against pathogens. However, the role of apoptosis inhibitor 5 (API5), in governing both ubiquitin-mediated autophagy and antiviral immunity, are poorly defined. Here, it is found that the serine/arginine-rich protein kinase 1 (SRPK1)-dependent phosphorylation of API5 at S464 site is essential for priming antiviral immune responses during diverse RNA virus infection. Mechanistically, phosphorylated API5 forms complexes with autophagic receptor p62 and eliminates itself from ubiquitination at K141, thereby reducing p62 aggregations and inhibiting the autophagic degradation of cytosolic RNA sensors RIG-I and MDA5 to mobilize RLR-mediated antiviral responses. Taken together, it is unveiled that API5 phosphorylation by SRPK1 is required for the inhibition of ubiquitin-mediated autophagic degradation of RNA sensors, revealing a coordinating nature of virus-host interactions that sustains host antiviral defenses.

Indexed as

Apoptosis Regulatory ProteinsDEAD Box Protein 58Host Microbial InteractionsInterferon-Induced Helicase, IFIH1Nuclear ProteinsRNA Virus InfectionsAnimalsAutophagyCell LineCytosolDisease Models, AnimalHumansInfluenza A Virus, H1N1 SubtypeMiceMice, Inbred C57BLMice, KnockoutApoptosis Regulatory ProteinsDEAD Box Protein 58Interferon-Induced Helicase, IFIH1Nuclear ProteinsProtein Serine-Threonine KinasesRNA, ViralSequestosome-1 ProteinAPI5 phosphorylationp62/SQSTM1RLR antiviral signalingubiquitin‐mediated autophagy

Identifiers

PMID40641422
PMCPMC12499447

What Socratic 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 Socratic graph.