Evidence map›Paper›PMID 26385923›Full record

ArticleThe Journal of biological chemistry2015

Structural Insights into mitochondrial antiviral signaling protein (MAVS)-tumor necrosis factor receptor-associated factor 6 (TRAF6) signaling.

Zhubing Shi, Zhen Zhang, Zhenzhen Zhang, Yanyan Wang, Chuanchuan Li, Xin Wang, Feng He, Lina Sun, Shi Jiao, Weiyang Shi and 1 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
1.2field-weighted citation impact, top 21% 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

32 citing papers in PubMed, 50 citations in OpenAlex.

  1. A Fish MDA5 Integrates Canonical RIG-I and MDA5 Ligand Recognition.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Article
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  4. Deubiquitinase OTULIN dampens RIG-I-dependent antiviral signaling by removing linear ubiquitination from TRAF6.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  5. Role of E5 from HPV16 in the Evasion of the Immune Response.International journal of molecular sciences · 2026
    Review
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  7. Review
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  12. Review
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  15. Article
  16. Article
  17. Article
  18. Advances in aquatic animal RIG-I-like receptors.Fish and shellfish immunology reports · 2021
    Review
  19. Article
  20. 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 at 5 institutions in 1 country.

Zhubing ShiFrom the School of Life Sciences and Technology, Tongji University, 1239 Siping Road, Shanghai 200092, China, the Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, State Key Laboratory of Cell Biology, Chinese Academy of Sciences, 320 Yue-Yang Road, Shanghai 200031, China, and.
Zhen Zhangthe Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, State Key Laboratory of Cell Biology, Chinese Academy of Sciences, 320 Yue-Yang Road, Shanghai 200031, China, and.
Zhenzhen Zhangthe Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, State Key Laboratory of Cell Biology, Chinese Academy of Sciences, 320 Yue-Yang Road, Shanghai 200031, China, and.
Yanyan Wangthe Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, State Key Laboratory of Cell Biology, Chinese Academy of Sciences, 320 Yue-Yang Road, Shanghai 200031, China, and.
Chuanchuan Lithe Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, State Key Laboratory of Cell Biology, Chinese Academy of Sciences, 320 Yue-Yang Road, Shanghai 200031, China, and.
Xin Wangthe Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, State Key Laboratory of Cell Biology, Chinese Academy of Sciences, 320 Yue-Yang Road, Shanghai 200031, China, and.
Feng Hethe Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, State Key Laboratory of Cell Biology, Chinese Academy of Sciences, 320 Yue-Yang Road, Shanghai 200031, China, and.
Lina SunQingdao Binhai University, Qingdao, Shandong 266555, China.
Shi Jiaothe Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, State Key Laboratory of Cell Biology, Chinese Academy of Sciences, 320 Yue-Yang Road, Shanghai 200031, China, and.
Weiyang ShiFrom the School of Life Sciences and Technology, Tongji University, 1239 Siping Road, Shanghai 200092, China, wshi@tongji.edu.cn.
Zhaocai Zhouthe Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, State Key Laboratory of Cell Biology, Chinese Academy of Sciences, 320 Yue-Yang Road, Shanghai 200031, China, and zczhou@sibcb.ac.cn.
Chinese Academy of Sciences · CNCenter for Excellence in Molecular Cell Science · CNShanghai Institutes for Biological Sciences · CNQingdao Binhai University · CNTongji University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In response to viral infection, cytosolic retinoic acid-inducible gene I-like receptors sense viral RNA and promote oligomerization of mitochondrial antiviral signaling protein (MAVS), which then recruits tumor necrosis factor receptor-associated factor (TRAF) family proteins, including TRAF6, to activate an antiviral response. Currently, the interaction between MAVS and TRAF6 is only partially understood, and atomic details are lacking. Here, we demonstrated that MAVS directly interacts with TRAF6 through its potential TRAF6-binding motif 2 (T6BM2; amino acids 455-460). Further, we solved the crystal structure of MAVS T6BM2 in complex with the TRAF6 TRAF_C domain at 2.95 Å resolution. T6BM2 of MAVS binds to the canonical adaptor-binding groove of the TRAF_C domain. Structure-directed mutational analyses in vitro and in cells revealed that MAVS binding to TRAF6 via T6BM2 instead of T6BM1 is essential but not sufficient for an optimal antiviral response. Particularly, a MAVS mutant Y460E retained its TRAF6-binding ability as predicted but showed significantly impaired signaling activity, highlighting the functional importance of this tyrosine. Moreover, these observations were further confirmed in MAVS(-/-) mouse embryonic fibroblast cells. Collectively, our work provides a structural basis for understanding the MAVS-TRAF6 antiviral response.

Indexed as

Adaptor Proteins, Signal TransducingAmino Acid SequenceAnimalsCrystallography, X-RayEscherichia coliFibroblastsGene ExpressionGenes, ReporterHEK293 CellsHost-Pathogen InteractionsHumansLuciferasesMiceMice, KnockoutMitochondriaMolecular Sequence DataAdaptor Proteins, Signal TransducingLuciferasesMAVS protein, humanRecombinant Fusion ProteinsTNF Receptor-Associated Factor 6Antiviral signalingcrystal structureinnate immunityMAVSprotein-protein interactionsignal transductionTNF receptor associated factor (TRAF)TRAF6

Identifiers

PMID26385923
PMCPMC4646334
OpenAlexW2240809217

What OpenQuestion holds

Textmetadata
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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.