ArticleJournal of cell science2014
TRIM15 is a focal adhesion protein that regulates focal adhesion disassembly.
Article in Journal of cell science, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
What it found
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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.
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.
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Who cites it
21 citing papers in PubMed, 27 citations in OpenAlex.
- TRIM15 Mediates ubiquitination of Paxillin to facilitate the progression of ovarian cancer.Cancer cell international · 2026Article
- EHD4 and ASAP2 are critical negative regulators of the claudin-5-based endothelial barrier.The FEBS journal · 2026Article
- Targeting TRIM15-mediated Axin1 depolymerization suppresses Wnt signaling and inhibits colorectal cancer growth.Cell death & disease · 2025Article
- Exploring the TRIM15 protein interaction network as a drug target using machine learning in pancreatic cancer.Discover oncology · 2025Article
- Identification of RING E3 pseudoligases in the TRIM protein family.Nature communications · 2025Article
- Exploring the role of the disulfidptosis-related gene SLC7A11 in adrenocortical carcinoma: implications for prognosis, immune infiltration, and therapeutic strategies.Cancer cell international · 2023Article
- Whole-genome DNA methylation and DNA methylation-based biomarkers in lung squamous cell carcinoma.iScience · 2023Article
- TRIM15 and CYLD regulate ERK activation via lysine-63-linked polyubiquitination.Nature cell biology · 2021Article
- Knockdown of TRIM15 inhibits the activation of hepatic stellate cells.Journal of molecular histology · 2021Article
- Cell-cell junctions: structure and regulation in physiology and pathology.Tissue barriers · 2021Review
- TRIM21 Polymorphisms are associated with Susceptibility and Clinical Status of Oral Squamous Cell Carcinoma patients.International journal of medical sciences · 2021Article
- Discriminating Origin Tissues of Tumor Cell Lines by Methylation Signatures and Dys-Methylated Rules.Frontiers in bioengineering and biotechnology · 2020Article
- Interleukin (IL)-22 from IL-20 Subfamily of Cytokines Induces Colonic Epithelial Cell Proliferation Predominantly through ERK1/2 Pathway.International journal of molecular sciences · 2019Article
- Rudhira/BCAS3 couples microtubules and intermediate filaments to promote cell migration for angiogenic remodeling.Molecular biology of the cell · 2019Article
- TRIM15 Exerts Anti-Tumor Effects Through Suppressing Cancer Cell Invasion in Gastric Adenocarcinoma.Medical science monitor : international medical journal of experimental and clinical research · 2018Article
- PTPN12/PTP-PEST Regulates Phosphorylation-Dependent Ubiquitination and Stability of Focal Adhesion Substrates in Invasive Glioblastoma Cells.Cancer research · 2018Article
- TRIM59 Is a Novel Marker of Poor Prognosis and Promotes Malignant Progression of Ovarian Cancer by Inducing Annexin A2 Expression.International journal of biological sciences · 2018Article
- Expression profiling of TRIM protein family in THP1-derived macrophages following TLR stimulation.Scientific reports · 2017Article
- The ubiquitin-proteasome system regulates focal adhesions at the leading edge of migrating cells.eLife · 2016Article
- Mmu-miR-1894-3p Inhibits Cell Proliferation and Migration of Breast Cancer Cells by Targeting Trim46.International journal of molecular sciences · 2016Article
Corrections and comments
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Authors and funding
14 authors at 2 institutions in 1 country.
Funding
Abstract
Focal adhesions are macromolecular complexes that connect the actin cytoskeleton to the extracellular matrix. Dynamic turnover of focal adhesions is crucial for cell migration. Paxillin is a multi-adaptor protein that plays an important role in regulating focal adhesion dynamics. Here, we identify TRIM15, a member of the tripartite motif protein family, as a paxillin-interacting factor and a component of focal adhesions. TRIM15 localizes to focal contacts in a myosin-II-independent manner by an interaction between its coiled-coil domain and the LD2 motif of paxillin. Unlike other focal adhesion proteins, TRIM15 is a stable focal adhesion component with restricted mobility due to its ability to form oligomers. TRIM15-depleted cells display impaired cell migration and reduced focal adhesion disassembly rates, in addition to enlarged focal adhesions. Thus, our studies demonstrate a cellular function for TRIM15 as a regulatory component of focal adhesion turnover and 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.