ArticlePloS one2013
Novel binding partners and differentially regulated phosphorylation sites clarify Eps8 as a multi-functional adaptor.
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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Who cites it
8 citing papers in PubMed, 13 citations in OpenAlex.
- Chlamydia repurposes the actin-binding protein EPS8 to disassemble epithelial tight junctions and promote infection.Cell host & microbe · 2022Article
- EPS8 phosphorylation by Src modulates its oncogenic functions.British journal of cancer · 2020Article
- Targeted therapies for non-HPV-related head and neck cancer: challenges and opportunities in the context of predictive, preventive, and personalized medicine.The EPMA journal · 2019Review
- Novel Nuclear Partnering Role of EPS8 With FOXM1 in Regulating Cell Proliferation.Frontiers in oncology · 2019Article
- Differential identity of Filopodia and Tunneling Nanotubes revealed by the opposite functions of actin regulatory complexes.Scientific reports · 2016Article
- Identification of HLA‑A*1101‑restricted cytotoxic T lymphocyte epitopes derived from epidermal growth factor pathway substrate number 8.Molecular medicine reports · 2016Article
- Regulation of Platelet Derived Growth Factor Signaling by Leukocyte Common Antigen-related (LAR) Protein Tyrosine Phosphatase: A Quantitative Phosphoproteomics Study.Molecular & cellular proteomics : MCP · 2016Article
- Eps8 controls Src- and FAK-dependent phenotypes in squamous carcinoma cells.Journal of cell science · 2014Article
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
Abstract
Eps8 is involved in both cell signalling and receptor trafficking. It is a known phosphorylation substrate for two proteins involved in the fibroblast growth factor receptor (FGFR) signalling pathway: the receptor itself and Src. Here we report a differential proteomic analysis of Eps8 aimed to identify specific FGFR and Src family kinase dependent phosphosites and co-associated phosphodependent binding partners. This study reveals a total of 22 Eps8 pTyr and pSer/Thr phosphorylation sites, including those that are dependent on Src family and FGFR kinase activity. Peptide affinity purification of proteins that bind to a selection of the pTyr phosphosites has identified a range of novel Eps8 binding partners including members of the intracellular vesicle trafficking machinery (clathrin and AP-2), proteins which have been shown to regulate activated receptor trafficking (NBR1 and Vav2), and proteins involved in receptor signalling (IRS4 and Shp2). Collectively this study significantly extends the understanding of Eps8 post-translational modification by regulated phosphorylation, identifies novel Eps8 binding partners implicated in receptor trafficking and signalling, and confirms the functions of Eps8 at the nexus of receptor signalling and vesicular trafficking.
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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.