The kinase Syk as an adaptor controlling sustained calcium signalling and B-cell development

EMBO J. 2008 May 7;27(9):1333-44. doi: 10.1038/emboj.2008.62. Epub 2008 Mar 27.

Abstract

Upon B-cell antigen receptor (BCR) activation, the protein tyrosine kinase Syk phosphorylates the adaptor protein SH2 domain-containing leukocyte protein of 65 kDa (SLP-65), thus coupling the BCR to diverse signalling pathways. Here, we report that SLP-65 is not only a downstream target and substrate of Syk but also a direct binding-partner and activator of this kinase. This positive feedback is mediated by the binding of the SH2 domain of SLP-65 to an autophosphorylated tyrosine of Syk. The mutant B cells that cannot form the Syk/SLP-65 complex are defective in BCR-induced extracellular signal-regulated kinase, nuclear factor kappa B and nuclear factor of activated T cells, but not Akt activation, and are blocked in B-cell development. Furthermore, we show that formation of the Syk/SLP-65 complex is required for sustained Ca(2+) responses in activated B cells. We suggest that after activation and internalization of the BCR, Syk remains active as part of a membrane-bound Syk/SLP-65 complex controlling sustained signalling and calcium influx.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adaptor Proteins, Signal Transducing / genetics
  • Adaptor Proteins, Signal Transducing / metabolism
  • Animals
  • Calcium / metabolism
  • Calcium Signaling / genetics
  • Calcium Signaling / physiology*
  • Cell Differentiation
  • Cell Line
  • Extracellular Signal-Regulated MAP Kinases / genetics
  • Extracellular Signal-Regulated MAP Kinases / metabolism
  • Flow Cytometry
  • Green Fluorescent Proteins / genetics
  • Green Fluorescent Proteins / metabolism
  • Intracellular Signaling Peptides and Proteins / genetics
  • Intracellular Signaling Peptides and Proteins / metabolism*
  • Luciferases / genetics
  • Luciferases / metabolism
  • Mice
  • Mice, Knockout
  • Models, Biological
  • Mutation
  • NF-kappa B / genetics
  • NF-kappa B / metabolism
  • Phosphorylation
  • Protein Binding
  • Protein-Tyrosine Kinases / genetics
  • Protein-Tyrosine Kinases / metabolism*
  • Proto-Oncogene Proteins c-akt / genetics
  • Proto-Oncogene Proteins c-akt / metabolism
  • Receptors, Antigen, B-Cell / genetics
  • Receptors, Antigen, B-Cell / metabolism*
  • Recombinant Fusion Proteins / genetics
  • Recombinant Fusion Proteins / metabolism
  • Syk Kinase
  • Transfection
  • Tyrosine / genetics
  • Tyrosine / metabolism
  • src Homology Domains / genetics

Substances

  • Adaptor Proteins, Signal Transducing
  • Intracellular Signaling Peptides and Proteins
  • NF-kappa B
  • Receptors, Antigen, B-Cell
  • Recombinant Fusion Proteins
  • Green Fluorescent Proteins
  • Tyrosine
  • Luciferases
  • Protein-Tyrosine Kinases
  • Syk Kinase
  • Syk protein, mouse
  • Proto-Oncogene Proteins c-akt
  • Extracellular Signal-Regulated MAP Kinases
  • Calcium