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Immunity. 2006 May;24(5):535-46.

Diacylglycerol and protein kinase D localization during T lymphocyte activation.

Author information

1
University of Dundee/WTB, Dow Street, Dundee DD2 1BE, United Kingdom. m.spitaler@imperial.ac.uk

Abstract

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.

PMID:
16713972
DOI:
10.1016/j.immuni.2006.02.013
[Indexed for MEDLINE]
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