Abstract 2318 Quantification of membrane protein assembly using SiMPull-POP
The EphA2 receptor acts to suppress tumorigenesis through binding of Ephrin-A ligands that cause receptor oligomerization, tyrosine autophosphorylation and kinase activity. Alternatively, EphA2 can promote tumor progression as it activates in the absence of ligand. However, the factors regulating EphA2 ligand-independent activity and its oligomeric state remain largely unknown. Current methodology used to assess protein-protein interactions lack the ability to quantitatively measure distinct oligomer populations, especially in a membrane environment.
Authors
- Ryan J Schuck (ORCID: https://orcid.org/0009-0009-1845-5277)
- Francisco Barrera (ORCID: https://orcid.org/0000-0001-5334-1528)
- Rajan Lamichhane (ORCID: https://orcid.org/0000-0003-0089-6452)
- Amita R. Sahoo (ORCID: https://orcid.org/0000-0002-2190-9518)
- Jennifer A. Rybak (ORCID: https://orcid.org/0000-0002-4017-0456)
- Alyssa Ward (ORCID: https://orcid.org/0000-0003-1321-3358)
- Ioannis Sgouralis (ORCID: https://orcid.org/0000-0001-7858-0197)
- R. Alexander Pyron (ORCID: https://orcid.org/0000-0003-2524-1794)
- Matthias Buck (ORCID: https://orcid.org/0000-0002-2958-0403)
Institutions
- Georgia Institute of Technology (US)
Publication Details
- Journal
- Journal of Biological Chemistry
- Published
- 2025-05-01
- DOI
- https://doi.org/10.1016/j.jbc.2025.109980
- Primary Topic
- RNA and protein synthesis mechanisms
- Type
- article
- Field-Weighted Citation Impact
- 0.00