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Nat Immunol. 2005 Feb;6(2):204-10. Epub 2005 Jan 16.

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

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Institute for Biology III, Albert-Ludwigs University of Freiburg and Max-Planck-Institute for Immunobiology, Stuebeweg 51, 79108 Freiburg, Germany.


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.

[Indexed for MEDLINE]

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