title: A leucine zipper in the N terminus confers membrane association to SLP-65.
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.
authors.affiliation: Institute for Biology III, Albert-Ludwigs University of Freiburg and Max-Planck-Institute for Immunobiology, Stuebeweg 51, 79108 Freiburg, Germany.
authors.forename: Fabian
authors.initials: F
authors.lastname: Köhler
authors.forename: Bettina
authors.initials: B
authors.lastname: Storch
authors.forename: Yogesh
authors.initials: Y
authors.lastname: Kulathu
authors.forename: Sebastian
authors.initials: S
authors.lastname: Herzog
authors.forename: Stephan
authors.initials: S
authors.lastname: Kuppig
authors.forename: Michael
authors.initials: M
authors.lastname: Reth
authors.forename: Hassan
authors.initials: H
authors.lastname: Jumaa
mesh_terms: D048868:Adaptor Proteins, Signal Transducing; D000595:Amino Acid Sequence; D000818:Animals; D002352:Carrier Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D002460:Cell Line; D002462:Cell Membrane / Q000378:metabolism*; D006801:Humans; D016350:Leucine Zippers; D051379:Mice; D008969:Molecular Sequence Data; D009154:Mutation / Q000235:genetics; D019814:Myristic Acid / Q000378:metabolism; D010750:Phosphoproteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D011485:Protein Binding; D021381:Protein Transport; D011947:Receptors, Antigen, B-Cell / Q000378:metabolism; D012441:Saccharomyces cerevisiae / Q000235:genetics / Q000378:metabolism; D016415:Sequence Alignment
chemical_list: D048868:Adaptor Proteins, Signal Transducing; C113939:B cell linker protein; D002352:Carrier Proteins; D010750:Phosphoproteins; D011947:Receptors, Antigen, B-Cell; C092947:SLP-76 signal Transducing adaptor proteins; D019814:Myristic Acid