PKCbeta modulates antigen receptor signaling via regulation of Btk membrane localization

EMBO J. 2001 Oct 15;20(20):5692-702. doi: 10.1093/emboj/20.20.5692.

Abstract

Mutations in Bruton's tyrosine kinase (Btk) result in X-linked agammaglobulinemia (XLA) in humans and X-linked immunodeficiency (xid) in mice. While targeted disruption of the protein kinase C-beta (PKCbeta) gene in mice results in an immunodeficiency similar to xid, the overall tyrosine phosphorylation of Btk is significantly enhanced in PKCbeta-deficient B cells. We provide direct evidence that PKCbeta acts as a feedback loop inhibitor of Btk activation. Inhibition of PKCbeta results in a dramatic increase in B-cell receptor (BCR)-mediated Ca2+ signaling. We identified a highly conserved PKCbeta serine phosphorylation site in a short linker within the Tec homology domain of Btk. Mutation of this phosphorylation site led to enhanced tyrosine phosphorylation and membrane association of Btk, and augmented BCR and FcepsilonRI-mediated signaling in B and mast cells, respectively. These findings provide a novel mechanism whereby reversible translocation of Btk/Tec kinases regulates the threshold for immunoreceptor signaling and thereby modulates lymphocyte activation.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • 3T3 Cells
  • Agammaglobulinaemia Tyrosine Kinase
  • Agammaglobulinemia / genetics
  • Alleles
  • Amino Acid Sequence
  • Animals
  • B-Lymphocytes / enzymology
  • B-Lymphocytes / immunology
  • Calcium Signaling / drug effects
  • Enzyme Activation
  • Enzyme Inhibitors / pharmacology
  • Feedback
  • Humans
  • Isoenzymes / antagonists & inhibitors
  • Isoenzymes / deficiency
  • Isoenzymes / genetics
  • Isoenzymes / physiology*
  • Lymphocyte Activation / physiology*
  • Mast Cells / enzymology
  • Mast Cells / immunology
  • Membrane Proteins / metabolism*
  • Mice
  • Mice, Knockout
  • Molecular Sequence Data
  • Mutagenesis, Site-Directed
  • Peptide Mapping
  • Phosphorylation
  • Phosphoserine / chemistry
  • Protein Kinase C / antagonists & inhibitors
  • Protein Kinase C / deficiency
  • Protein Kinase C / genetics
  • Protein Kinase C / physiology*
  • Protein Kinase C beta
  • Protein Processing, Post-Translational
  • Protein Structure, Tertiary
  • Protein Transport
  • Protein-Tyrosine Kinases / chemistry
  • Protein-Tyrosine Kinases / metabolism*
  • Receptors, Antigen, B-Cell / physiology*
  • Receptors, IgE / physiology

Substances

  • Enzyme Inhibitors
  • Isoenzymes
  • Membrane Proteins
  • Receptors, Antigen, B-Cell
  • Receptors, IgE
  • Phosphoserine
  • Tec protein-tyrosine kinase
  • Protein-Tyrosine Kinases
  • Agammaglobulinaemia Tyrosine Kinase
  • BTK protein, human
  • Btk protein, mouse
  • Protein Kinase C
  • Protein Kinase C beta