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  Structurally encoded intraclass differences in EphA clusters drive distinct cell responses

Seiradake, E., Schaupp, A., Del Toro Ruiz, D., Kaufmann, R., Mitakidis, N., Harlos, K., et al. (2013). Structurally encoded intraclass differences in EphA clusters drive distinct cell responses. NATURE STRUCTURAL & MOLECULAR BIOLOGY, 20(8), 958-964. doi:10.1038/nsmb.2617.

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Seiradake, Elena1, Autor
Schaupp, Andreas2, Autor           
Del Toro Ruiz, Daniel2, Autor           
Kaufmann, Rainer1, Autor
Mitakidis, Nikolaos1, Autor
Harlos, Karl1, Autor
Aricescu, A. Radu1, Autor
Klein, Rüdiger2, Autor           
Jones, E. Yvonne1, Autor
Affiliations:
1external, ou_persistent22              
2Department: Molecules–Signaling–Development / Klein, MPI of Neurobiology, Max Planck Society, ou_1113546              

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Schlagwörter: MAXIMUM-LIKELIHOOD; DIFFRACTION DATA; RECEPTORS; EPHRINS; CANCER; CRYSTALLIZATION; RESOLUTION; REFINEMENT; EXPRESSION; MIGRATION
 Zusammenfassung: 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 of EphA4 ectodomain alone and in complexes with ephrinB3 and ephrinA5. These revealed closed clusters with a dimeric or circular arrangement in the crystal lattice, contrasting with extended arrays previously observed for EphA2 ectodomain. Localization microscopy showed that ligand-stimulated EphA4 induces smaller clusters than does EphA2. Mutant Ephs link these characteristics to interactions observed in the crystal lattices, suggesting a mechanism by which distinctive ectodomain surfaces determine clustering, and thereby signaling, properties.

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Sprache(n): eng - English
 Datum: 2013-08
 Publikationsstatus: Erschienen
 Seiten: 9
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: -
 Identifikatoren: ISI: 000322715300009
DOI: 10.1038/nsmb.2617
 Art des Abschluß: -

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Titel: NATURE STRUCTURAL & MOLECULAR BIOLOGY
Genre der Quelle: Zeitschrift
 Urheber:
Affiliations:
Ort, Verlag, Ausgabe: 75 VARICK ST, 9TH FLR, NEW YORK, NY 10013-1917 USA : NATURE PUBLISHING GROUP
Seiten: - Band / Heft: 20 (8) Artikelnummer: - Start- / Endseite: 958 - 964 Identifikator: ISSN: 1545-9993