ArticleThe Journal of biological chemistry2014
Binding and function of phosphotyrosines of the Ephrin A2 (EphA2) receptor using synthetic sterile α motif (SAM) domains.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
What it found
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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
11 citing papers in PubMed.
- Eph receptor signaling complexes in the plasma membrane.Trends in biochemical sciences · 2024Review
- PHB2 promotes SHIP2 ubiquitination via the E3 ligase NEDD4 to regulate AKT signaling in gastric cancer.Journal of experimental & clinical cancer research : CR · 2024Article
- Eph Receptors in Cancer.Biomedicines · 2023Review
- Hunting for Novel Routes in Anticancer Drug Discovery: Peptides against Sam-Sam Interactions.International journal of molecular sciences · 2022Review
- The intracellular domains of the EphB6 and EphA10 receptor tyrosine pseudokinases function as dynamic signalling hubs.The Biochemical journal · 2021Article
- Quantitative Tyrosine Phosphoproteome Profiling of AXL Receptor Tyrosine Kinase Signaling Network.Cancers · 2021Article
- Review
- A role of the SAM domain in EphA2 receptor activation.Scientific reports · 2017Article
- The SAM domain inhibits EphA2 interactions in the plasma membrane.Biochimica et biophysica acta. Molecular cell research · 2017Article
- Association between polymorphisms of OGG1, EPHA2 and age-related cataract risk: a meta-analysis.BMC ophthalmology · 2016Article
- PIPThe Journal of biological chemistryArticle
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
The sterile α motif (SAM) domain of the ephrin receptor tyrosine kinase, EphA2, undergoes tyrosine phosphorylation, but the effect of phosphorylation on the structure and interactions of the receptor is unknown. Studies to address these questions have been hindered by the difficulty of obtaining site-specifically phosphorylated proteins in adequate amounts. Here, we describe the use of chemically synthesized and specifically modified domain-length peptides to study the behavior of phosphorylated EphA2 SAM domains. We show that tyrosine phosphorylation of any of the three tyrosines, Tyr(921), Tyr(930), and Tyr(960), has a surprisingly small effect on the EphA2 SAM structure and stability. However, phosphorylation at Tyr(921) and Tyr(930) enables differential binding to the Src homology 2 domain of the adaptor protein Grb7, which we propose will lead to distinct functional outcomes. Setting up different signaling platforms defined by selective interactions with adaptor proteins thus adds another level of regulation to EphA2 signaling.
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Registered trials
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