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  A leucine zipper in the N terminus confers membrane association to SLP-65

Köhler, F., Storch, B., Kulathu, Y., Herzog, S., Kuppig, S., Reth, M., et al. (2005). A leucine zipper in the N terminus confers membrane association to SLP-65. Nature Immunology, 6, 204-210.

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Datensatz-Permalink: https://hdl.handle.net/11858/00-001M-0000-002B-9337-F Versions-Permalink: https://hdl.handle.net/11858/00-001M-0000-002B-9338-D
Genre: Zeitschriftenartikel

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 Urheber:
Köhler, Fabian1, Autor           
Storch, Bettina1, Autor           
Kulathu, Yogesh1, Autor           
Herzog, Sebastian1, Autor           
Kuppig, Stephan1, Autor           
Reth, Michael1, Autor           
Jumaa, Hassan1, Autor           
Affiliations:
1Research Group and Chair of Molecular Immunology of the University of Freiburg, Max Planck Institute of Immunobiology and Epigenetics, Max Planck Society, ou_2243645              

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 Zusammenfassung: Membrane recruitment of adaptor proteins is crucial for coupling antigen receptors to downstream signaling events. Despite the essential function of the B cell adaptor SLP-65, the mechanism of its recruitment to the plasma membrane is not yet understood. Here we show that a highly conserved leucine zipper in the SLP-65 N terminus is responsible for membrane association. Alterations in the N terminus abolished SLP-65 membrane localization and activity, both of which were restored by replacement of the N terminus with a myristoylation signal. The N terminus is an autonomous domain that confers specific localization and function when transferred to green fluorescent protein or the adaptor protein SLP-76. Our data elucidate the mechanism of SLP-65 membrane recruitment and suggest that leucine zipper motifs are essential interaction domains of signaling proteins.

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Sprache(n): eng - English
 Datum: 2005-02
 Publikationsstatus: Erschienen
 Seiten: -
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: Expertenbegutachtung
 Identifikatoren: eDoc: 263308
 Art des Abschluß: -

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Titel: Nature Immunology
Genre der Quelle: Zeitschrift
 Urheber:
Affiliations:
Ort, Verlag, Ausgabe: -
Seiten: - Band / Heft: 6 Artikelnummer: - Start- / Endseite: 204 - 210 Identifikator: -