Evidence map›Paper›PMID 19465916›Full record

ArticleNature structural & molecular biology2009

E2 interaction and dimerization in the crystal structure of TRAF6.

Qian Yin, Su-Chang Lin, Betty Lamothe, Miao Lu, Yu-Chih Lo, Gregory Hura, Lixin Zheng, Rebecca L Rich, Alejandro D Campos, David G Myszka and 3 more

Open access · greenAbstract read
In one paragraph

Article in Nature structural & molecular biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 211 papers.

0numbers the graph read from it
0cells of the map it votes in
211citing papers in PubMed
8.4field-weighted citation impact, top 2% 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

211 citing papers in PubMed, 346 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. TRAF6 coiled-coil domain mediates its trimerization.bioRxiv : the preprint server for biology · 2025
    Article
  8. Article
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  12. Article
  13. Article
  14. Article
  15. Review
  16. Review
  17. Article
  18. Article
  19. TIFAB regulates the TIFA-TRAF6 signaling pathway involved in innate immunity by forming a heterodimer complex with TIFA.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  20. Article

151 more citing papers are in PubMed but not listed here.

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

13 authors at 6 institutions in 1 country.

Qian YinWeill Medical College of Cornell University, New York, New York, USA.
Su-Chang Lin
Betty Lamothe
Miao Lu
Yu-Chih Lo
Gregory Hura
Lixin Zheng
Rebecca L Rich
Alejandro D Campos
David G Myszka
Michael J Lenardo
Bryant G Darnay
Hao Wu
Cornell University · USThe University of Texas MD Anderson Cancer Center · USNational Institutes of Health · USUniversity of Utah · USLawrence Berkeley National Laboratory · USTri-Institutional PhD Program in Chemical Biology · US

Funding

Molecular Mechanisms and Treatment Of Autoimmunity In Man And Animal ModelsZIAAI000717 · NIAID · NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES · PI SU, HELEN CHUN-HUI · 2009 to 2025
$13.2M
Structural Studies of TNF Receptor Associated Factors (TRAFs)R01AI045937 · NIAID · WEILL MEDICAL COLL OF CORNELL UNIV · PI WU, HAO · 1999 to 2016
$5.9M
TRAF6 E3 LIGASE FUNCTION IN OSTEOCLASTOGENESISR01AR053540 · NIAMS · UNIVERSITY OF TX MD ANDERSON CAN CTR · PI DARNAY, BRYANT G · 2007 to 2010
$852k
Intramural NIH HHSNIAID NIH HHS R01 AI045937NIAMS NIH HHS R01 AR053540
6 · The paper itself

Abstract

Tumor necrosis factor (TNF) receptor-associated factor (TRAF)-6 mediates Lys63-linked polyubiquitination for NF-kappaB activation via its N-terminal RING and zinc finger domains. Here we report the crystal structures of TRAF6 and its complex with the ubiquitin-conjugating enzyme (E2) Ubc13. The RING and zinc fingers of TRAF6 assume a rigid, elongated structure. Interaction of TRAF6 with Ubc13 involves direct contacts of the RING and the preceding residues, and the first zinc finger has a structural role. Unexpectedly, this region of TRAF6 is dimeric both in the crystal and in solution, different from the trimeric C-terminal TRAF domain. Structure-based mutagenesis reveals that TRAF6 dimerization is crucial for polyubiquitin synthesis and autoubiquitination. Fluorescence resonance energy transfer analysis shows that TRAF6 dimerization induces higher-order oligomerization of full-length TRAF6. The mismatch of dimeric and trimeric symmetry may provide a mode of infinite oligomerization that facilitates ligand-dependent signal transduction of many immune receptors.

Indexed as

Crystallography, X-RayFluorescence Resonance Energy TransferHumansProtein ConformationProtein MultimerizationRING Finger DomainsTNF Receptor-Associated Factor 6UbiquitinationUbiquitin-Conjugating EnzymesZinc FingersTNF Receptor-Associated Factor 6UBE2N protein, humanUbiquitin-Conjugating Enzymes

Identifiers

PMID19465916
PMCPMC2834951
OpenAlexW2147005308

What OpenQuestion holds

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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.