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

Fabian Köhler; Bettina Storch; Yogesh Kulathu; Sebastian Herzog; Stephan Kuppig; Michael Reth; Hassan Jumaa

doi:10.1038/ni1163

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

Fabian Köhler
, Bettina Storch
, Yogesh Kulathu
, Sebastian Herzog
, Stephan Kuppig
, Michael Reth
, Hassan Jumaa

MRC PPU

Research output: Contribution to journal › Article › peer-review

48 Citations (Scopus)

Abstract

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.

Original language	English
Pages (from-to)	204-210
Number of pages	7
Journal	Nature Immunology
Volume	6
Issue number	2
DOIs	https://doi.org/10.1038/ni1163
Publication status	Published - 1 Feb 2005

ASJC Scopus subject areas

Immunology and Allergy
Immunology

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abstract = "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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AU - Köhler, Fabian

AU - Storch, Bettina

AU - Kulathu, Yogesh

AU - Herzog, Sebastian

AU - Kuppig, Stephan

AU - Reth, Michael

AU - Jumaa, Hassan

PY - 2005/2/1

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N2 - 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.

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

Abstract

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