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

Nat Immunol. 2005 Feb;6(2):204-10. doi: 10.1038/ni1163. Epub 2005 Jan 16.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adaptor Proteins, Signal Transducing
  • Amino Acid Sequence
  • Animals
  • Carrier Proteins / chemistry*
  • Carrier Proteins / genetics
  • Carrier Proteins / metabolism*
  • Cell Line
  • Cell Membrane / metabolism*
  • Humans
  • Leucine Zippers*
  • Mice
  • Molecular Sequence Data
  • Mutation / genetics
  • Myristic Acid / metabolism
  • Phosphoproteins / chemistry*
  • Phosphoproteins / genetics
  • Phosphoproteins / metabolism*
  • Protein Binding
  • Protein Transport
  • Receptors, Antigen, B-Cell / metabolism
  • Saccharomyces cerevisiae / genetics
  • Saccharomyces cerevisiae / metabolism
  • Sequence Alignment

Substances

  • Adaptor Proteins, Signal Transducing
  • B cell linker protein
  • Carrier Proteins
  • Phosphoproteins
  • Receptors, Antigen, B-Cell
  • SLP-76 signal Transducing adaptor proteins
  • Myristic Acid