Comment on "PDK1 nucleates T cell receptor-induced signaling complex for NF-kappaB activation"

Science. 2006 Apr 7;312(5770):55; author reply 55. doi: 10.1126/science.1122000.

Abstract

We observe that protein kinase C (PKC) is phosphorylated on the activation loop at threonine 538 (Thr-538) before T cell activation. Our results are inconsistent with the conclusions of Lee et al. (Reports, 1 April 2005, p. 114) that the Thr-538 phosphorylation of PKC is regulated by T cell receptor activation. Other mechanisms, such as autophosphorylation of Thr-219, might orchestrate the cellular function of PKC in T cells.

Publication types

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

MeSH terms

  • 3-Phosphoinositide-Dependent Protein Kinases
  • Animals
  • Antibodies / immunology
  • CD28 Antigens / immunology
  • CD3 Complex / immunology
  • Cells, Cultured
  • Humans
  • Isoenzymes / metabolism*
  • Jurkat Cells
  • Lymphocyte Activation
  • Mice
  • NF-kappa B / metabolism*
  • Phosphorylation
  • Protein Kinase C / metabolism*
  • Protein Kinase C-theta
  • Protein-Serine-Threonine Kinases / metabolism*
  • Receptors, Antigen, T-Cell / metabolism
  • Signal Transduction
  • T-Lymphocytes / enzymology
  • T-Lymphocytes / immunology
  • T-Lymphocytes / metabolism*
  • Threonine / metabolism

Substances

  • Antibodies
  • CD28 Antigens
  • CD3 Complex
  • Isoenzymes
  • NF-kappa B
  • Receptors, Antigen, T-Cell
  • Threonine
  • 3-Phosphoinositide-Dependent Protein Kinases
  • PDPK1 protein, human
  • Pdpk1 protein, mouse
  • Protein-Serine-Threonine Kinases
  • PRKCQ protein, human
  • Prkcq protein, mouse
  • Protein Kinase C
  • Protein Kinase C-theta