Ephrin‐As, Eph receptors and integrin α3 interact and colocalise at membrane protrusions of U251MG glioblastoma cells

• DOI: 10.1002/cbin.10134
• Publication Date: 2013-08-06T09:42:11Z
• Authors: Andrey Makarov; Irene Ylivinkka; Tuula A. Nyman; Marko Hyytiäinen; Jorma Keski‐Oja
• Keywords: Ephrin; EPH receptor A2

Glioblastoma is the most common brain cancer. Ephrins and their Eph receptors play important roles in development of central nervous system regulation cancer cell migration invasion. In a search for receptor complexes, we used tandem affinity purification based interaction screening with tagged ephrins A1, A3 A4 combined protein identification by mass-spectrometry U251MG glioblastoma cells. bound to receptors, mainly EphA2 these Integrin α3 was identified complexes ephrin-As. Soluble ephrin-A1 colocalised integrin at surface, rapidly endocytosed However, did not colocalise internalised ephrin-A1, whereas did. cells, edges protrusions. Sites EphA2-integrin colocalisation were positive vinculin, focal adhesion kinase phosphotyrosine, that is, markers active signalling. The between ephrin-As, plausibly crosstalk signalling pathways membrane protrusions