Structurally encoded intraclass differences in EphA clusters drive distinct cell responses.

Journal article

Functional outcomes of ephrin binding to Eph receptors (Ephs) range from cell repulsion to adhesion. Here we used cell collapse and stripe assays, showing contrasting effects of human ephrinA5 binding to EphA2 and EphA4. Despite equivalent ligand binding affinities, EphA4 triggered greater cell collapse, whereas EphA2-expressing cells adhered better to ephrinA5-coated surfaces. Chimeric receptors showed that the ectodomain is a major determinant of cell response. We report crystal structures ...

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Authors: Seiradake, E; Schaupp, A; del Toro Ruiz, D; Kaufmann, R; Mitakidis, N

• Publication status: Published
• Journal: Nature structural and molecular biology
• Volume: 20
• Issue: 8
• Pages: 958-964
• Publication date: 2013-08-01
• DOI: 10.1038/nsmb.2617
• EISSN: 1545-9985
• ISSN: 1545-9993
• Language: English
• Keywords: Crystallography, X-Ray; Models, Molecular; Recombinant Fusion Proteins; Hela Cells; Animals; Microscopy, Fluorescence; Receptors, Eph Family; Protein Conformation; Mice; HEK293 Cells; Humans; COS Cells; Multiprotein Complexes; Cercopithecus aethiops