Diacylglycerol and protein kinase D localization during T lymphocyte activation

Martin Spitaler, Elizabeth Emslie, C. David Wood, Doreen Cantrell

    Research output: Contribution to journalArticlepeer-review

    94 Citations (Scopus)


    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.
    Original languageEnglish
    Pages (from-to)535-546
    Number of pages12
    Issue number5
    Publication statusPublished - 2006


    • T lymphocytes
    • Protein kinase


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