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 |
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Pages (from-to) | 204-210 |
Number of pages | 7 |
Journal | Nature Immunology |
Volume | 6 |
Issue number | 2 |
DOIs | |
Publication status | Published - 1 Feb 2005 |
ASJC Scopus subject areas
- Immunology and Allergy
- Immunology