Diacylglycerol and protein kinase D localization during T lymphocyte activation

Immunity. 2006 May;24(5):535-46. doi: 10.1016/j.immuni.2006.02.013.


The serine kinase protein kinase D (PKD) has a cysteine-rich domain (CRD) that binds diacylglycerol (DAG) with high affinity. PKD is cytosolic in unstimulated T cells, but it rapidly polarizes to the immunological synapse in response to antigen/antigen presenting cells (APCs). PKD repositioning is determined by the accumulation of DAG at the immunological synapse and changes in DAG accessibility of the PKD-CRD. Unstimulated T cells are shown to have a uniform distribution of DAG at the plasma membrane, whereas after T cell activation, a gradient of DAG is created with a persistent focus of DAG at the center of the synapse. PKD is only transiently associated with the immune synapse, indicating a fine tuning of PKD responsiveness to DAG by additional regulatory mechanisms. These results reveal the immune synapse as a focal point for DAG and PKD as an immediate and dynamic DAG effector during T cell activation.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Diglycerides / immunology*
  • Diglycerides / metabolism
  • Flow Cytometry
  • Humans
  • Image Processing, Computer-Assisted
  • Jurkat Cells
  • Lymphocyte Activation / immunology*
  • Microscopy, Confocal
  • Protein Kinase C / immunology*
  • Protein Kinase C / metabolism
  • Receptors, Antigen, T-Cell
  • Signal Transduction / immunology*
  • T-Lymphocytes / immunology*
  • T-Lymphocytes / metabolism
  • Transfection


  • Diglycerides
  • Receptors, Antigen, T-Cell
  • protein kinase D
  • Protein Kinase C