ArticleProceedings of the National Academy of Sciences of the United States of America2017
Molecular basis for unique specificity of human TRAF4 for platelets GPIbβ and GPVI.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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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.
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Who cites it
9 citing papers in PubMed, 15 citations in OpenAlex.
- TRAF6 coiled-coil domain mediates its trimerization.bioRxiv : the preprint server for biology · 2025Article
- TRAF1 from a Structural Perspective.Biomolecules · 2024Review
- Signaling mechanisms of the platelet glycoprotein Ib-IX complex.Platelets · 2022Review
- TNF receptor agonists induce distinct receptor clusters to mediate differential agonistic activity.Communications biology · 2021Article
- Structural feature of TRAFs, their related human diseases and therapeutic intervention.Archives of pharmacal research · 2021Review
- Comparison of Target Recognition by TRAF1 and TRAF2.International journal of molecular sciences · 2020Article
- TRAF4 binds to the juxtamembrane region of EGFR directly and promotes kinase activation.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- In Vitro Inhibitory Mechanism Effect of TRAIP on the Function of TRAF2 Revealed by Characterization of Interaction Domains.International journal of molecular sciences · 2018Article
- Structure of TRAF Family: Current Understanding of Receptor Recognition.Frontiers in immunology · 2018Review
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Tumor necrosis factor (TNF)-receptor associated factor 4 (TRAF4), an adaptor protein with E3-ligase activity, is involved in embryogenesis, cancer initiation and progression, and platelet receptor (GPIb-IX-V complex and GPVI)-mediated signaling for reactive oxygen species (ROS) production that initiates thrombosis at arterial shears. Disruption of platelet receptors and the TRAF4 interaction is a potential target for therapeutic intervention by antithrombotic drugs. Here, we report a crystal structure of TRAF4 (amino acid residues 290∼470) in complex with a peptide from the GPIbβ receptor (amino acid residues 177∼181). The GPIbβ peptide binds to a unique shallow surface composed of two hydrophobic pockets on TRAF4. Further studies revealed the TRAF4-binding motif Arg-Leu-X-Ala. The TRAF4-binding motif was present not only in platelet receptors but also in the TGF-β receptor. The current structure will provide a template for furthering our understanding of the receptor-binding specificity of TRAF4, TRAF4-mediated signaling, and related diseases.
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Registered trials
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.