ArticleOncogene2002
Cloning of a novel phosphotyrosine binding domain containing molecule, Odin, involved in signaling by receptor tyrosine kinases.
Article in Oncogene, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 45 citations in OpenAlex.
- The Structural Dynamics, Complexity of Interactions, and Functions in Cancer of Multi-SAM Containing Proteins.Cancers · 2023Review
- Confirmation of five novel susceptibility loci for systemic lupus erythematosus (SLE) and integrated network analysis of 82 SLE susceptibility loci.Human molecular genetics · 2017Article
- Anks1a regulates COPII-mediated anterograde transport of receptor tyrosine kinases critical for tumorigenesis.Nature communications · 2016Article
- In Vivo Expression of the PTB-deleted Odin Mutant Results in Hydrocephalus.Molecules and cells · 2015Article
- Combinatorial proteomic analysis of intercellular signaling applied to the CD28 T-cell costimulatory receptor.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Article
- EGF receptor trafficking: consequences for signaling and cancer.Trends in cell biology · 2014Review
- Article
- Global proteomic assessment of the classical protein-tyrosine phosphatome and "Redoxome".Cell · 2011Article
- The interactome of a PTB domain-containing adapter protein, Odin, revealed by SILAC.Journal of proteomics · 2011Article
- The SAM domains of Anks family proteins are critically involved in modulating the degradation of EphA receptors.Molecular and cellular biology · 2010Article
- Insertional mutagenesis in mice deficient for p15Ink4b, p16Ink4a, p21Cip1, and p27Kip1 reveals cancer gene interactions and correlations with tumor phenotypes.Cancer research · 2010Article
- Biotin tagging coupled with amino acid-coded mass tagging for efficient and precise screening of interaction proteome in mammalian cells.Proteomics · 2009Article
- Odin (ANKS1A) is a Src family kinase target in colorectal cancer cells.Cell communication and signaling : CCS · 2008Article
- Identification of phosphotyrosine binding domain-containing proteins as novel downstream targets of the EphA8 signaling function.Molecular and cellular biology · 2007Article
- Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.Nature biotechnology · 2005Article
- Temporal analysis of phosphotyrosine-dependent signaling networks by quantitative proteomics.Nature biotechnology · 2004Article
- Cloning of a novel signaling molecule, AMSH-2, that potentiates transforming growth factor beta signaling.BMC cell biology · 2004Article
Corrections and comments
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Authors and funding
11 authors at 4 institutions in 4 countries.
Funding
Abstract
We have used a proteomic approach using mass spectrometry to identify signaling molecules involved in receptor tyrosine kinase signaling pathways. Using affinity purification by anti-phosphotyrosine antibodies to enrich for tyrosine phosphorylated proteins, we have identified a novel signaling molecule in the epidermal growth factor receptor signaling pathway. This molecule, designated Odin, contains several ankyrin repeats, two sterile alpha motifs and a phosphotyrosine binding domain and is ubiquitously expressed. Using antibodies against endogenous Odin, we show that it undergoes tyrosine phosphorylation upon addition of growth factors such as EGF or PDGF but not by cytokines such as IL-3 or erythropoietin. Immunofluorescence experiments as well as Western blot analysis on subcellular fractions demonstrated that Odin is localized to the cytoplasm both before and after growth factor treatment. Deletion analysis showed that the phosphotyrosine binding domain of Odin is not required for its tyrosine phosphorylation. Overexpression of Odin, but not an unrelated adapter protein, Grb2, inhibited EGF-induced activation of c-Fos promoter. Microinjection of wild-type or a mutant version lacking the PTB domain into NIH3T3 fibroblasts inhibited PDGF-induced mitogenesis. Taken together, our results indicate that Odin may play a negative role in growth factor receptor signaling pathways.
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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.