ArticlePLoS biology2013
TRAF4 is a novel phosphoinositide-binding protein modulating tight junctions and favoring cell migration.
Article in PLoS biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 51 citations in OpenAlex.
- TRAF6 coiled-coil domain mediates its trimerization.bioRxiv : the preprint server for biology · 2025Article
- Combining Network Pharmacology, Molecular Docking, and Integrative Studies to Explore the Mechanism ofFood science & nutrition · 2025Article
- TRAF1 from a Structural Perspective.Biomolecules · 2024Review
- TRAF4 is crucial for ST2+ memory Th2 cell expansion in IL-33-driven airway inflammation.JCI insight · 2023Article
- SRC-3/TRAF4 facilitates ovarian cancer development by activating the PI3K/AKT signaling pathway.Medical oncology (Northwood, London, England) · 2023Article
- Transmembrane Membrane Readers form a Novel Class of Proteins That Include Peripheral Phosphoinositide Recognition Domains and Viral Spikes.Membranes · 2022Review
- TRAF4 Promotes the Proliferation of Glioblastoma by Stabilizing SETDB1 to Activate the AKT Pathway.International journal of molecular sciences · 2022Article
- The Research Progress in Physiological and Pathological Functions of TRAF4.Frontiers in oncology · 2022Review
- Article
- Structural feature of TRAFs, their related human diseases and therapeutic intervention.Archives of pharmacal research · 2021Review
- Article
- The type 2 diabetes gene product STARD10 is a phosphoinositide-binding protein that controls insulin secretory granule biogenesis.Molecular metabolism · 2020Article
- A Genetic Screen inG3 (Bethesda, Md.) · 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
- Phosphoinositides and Membrane Targeting in Cell Polarity.Cold Spring Harbor perspectives in biology · 2018Review
- Peripheral Nerve Injury Induces Dynamic Changes of Tight Junction Components.Frontiers in physiology · 2018Article
- Genetic Alterations of TRAF Proteins in Human Cancers.Frontiers in immunology · 2018Review
- Structure of TRAF Family: Current Understanding of Receptor Recognition.Frontiers in immunology · 2018Review
- Polarity and morphogenesis of the eye epithelium requires the adhesion junction associated adaptor protein Traf4.Cell adhesion & migration · 2018Article
- DnaA and LexA Proteins Regulate Transcription of theFrontiers in microbiology · 2018Article
Corrections and comments
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Authors and funding
8 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Tumor necrosis factor (TNF) receptor-associated factor 4 (TRAF4) is frequently overexpressed in carcinomas, suggesting a specific role in cancer. Although TRAF4 protein is predominantly found at tight junctions (TJs) in normal mammary epithelial cells (MECs), it accumulates in the cytoplasm of malignant MECs. How TRAF4 is recruited and functions at TJs is unclear. Here we show that TRAF4 possesses a novel phosphoinositide (PIP)-binding domain crucial for its recruitment to TJs. Of interest, this property is shared by the other members of the TRAF protein family. Indeed, the TRAF domain of all TRAF proteins (TRAF1 to TRAF6) is a bona fide PIP-binding domain. Molecular and structural analyses revealed that the TRAF domain of TRAF4 exists as a trimer that binds up to three lipids using basic residues exposed at its surface. Cellular studies indicated that TRAF4 acts as a negative regulator of TJ and increases cell migration. These functions are dependent from its ability to interact with PIPs. Our results suggest that TRAF4 overexpression might contribute to breast cancer progression by destabilizing TJs and favoring cell migration.
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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.