ArticleBiochimica et biophysica acta. Molecular cell research2017
The SAM domain inhibits EphA2 interactions in the plasma membrane.
Article in Biochimica et biophysica acta. Molecular cell research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed, 59 citations in OpenAlex.
- miR-1297 is frequently downmodulated in flat epithelial atypia of the breast and promotes mammary neoplastic transformation via EphrinA2 regulation.Journal of experimental & clinical cancer research : CR · 2025Article
- Sam-Sam Association Between EphA2 and SASH1: In Silico Studies of Cancer-Linked Mutations.Molecules (Basel, Switzerland) · 2025Article
- Eph receptor signaling complexes in the plasma membrane.Trends in biochemical sciences · 2024Review
- Article
- Probing phosphorylation events in biological membranes: The transducer function.Biochimica et biophysica acta. Biomembranes · 2024Review
- Transmembrane helix interactions regulate oligomerization of the receptor tyrosine kinase EphA2.The Journal of biological chemistry · 2024Article
- Co-clustering of EphB6 and ephrinB1 in trans restrains cancer cell invasion.Communications biology · 2024Article
- Cancer-Related Mutations in the Sam Domains of EphA2 Receptor and Ship2 Lipid Phosphatase: A Computational Study.Molecules (Basel, Switzerland) · 2024Article
- Optogenetic Regulation of EphA1 RTK Activation and Signaling.bioRxiv : the preprint server for biology · 2024Article
- Abnormal function ofInternational journal of ophthalmology · 2024Article
- Ephrin-Eph receptor tyrosine kinases for potential therapeutics against hepatic pathologies.Journal of cell communication and signaling · 2023Review
- Sticky, Adaptable, and Many-sided: SAM protein versatility in normal and pathological hematopoietic states.BioEssays : news and reviews in molecular, cellular and developmental biology · 2023Review
- 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
- Ligands with different dimeric configurations potently activate the EphA2 receptor and reveal its potential for biased signaling.iScience · 2022Article
- Article
- Conformational Clamping by a Membrane Ligand Activates the EphA2 Receptor.Journal of molecular biology · 2021Article
- A cancer mutation promotes EphA4 oligomerization and signaling by altering the conformation of the SAM domain.The Journal of biological chemistry · 2021Article
- Probing Membrane Protein Association Using Concentration-Dependent Number and Brightness.Angewandte Chemie (International ed. in English) · 2021Article
- The Biased Ligands NGF and NT-3 Differentially Stabilize Trk-A Dimers.Biophysical journal · 2021Article
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
All members of the Eph receptor family of tyrosine kinases contain a SAM domain near the C terminus, which has been proposed to play a role in receptor homotypic interactions and/or interactions with binding partners. The SAM domain of EphA2 is known to be important for receptor function, but its contribution to EphA2 lateral interactions in the plasma membrane has not been determined. Here we use a FRET-based approach to directly measure the effect of the SAM domain on the stability of EphA2 dimers on the cell surface in the absence of ligand binding. We also investigate the functional consequences of EphA2 SAM domain deletion. Surprisingly, we find that the EphA2 SAM domain inhibits receptor dimerization and decreases EphA2 tyrosine phosphorylation. This role is dramatically different from the role of the SAM domain of the related EphA3 receptor, which we previously found to stabilize EphA3 dimers and increase EphA3 tyrosine phosphorylation in cells in the absence of ligand. Thus, the EphA2 SAM domain likely contributes to a unique mode of EphA2 interaction that leads to distinct signaling outputs.
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