Diacylglycerol and protein kinase D localization during T lymphocyte activation.

Spitaler, Martin, Emslie, Elisabeth, Wood, C David and Cantrell, Doreen (2006) Diacylglycerol and protein kinase D localization during T lymphocyte activation. Immunity, 24 (5). pp. 535-546. ISSN 1074-7613

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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.

Item Type: Article
Schools and Departments: School of Life Sciences > Biochemistry
Subjects: Q Science
Related URLs:
Depositing User: David Wood
Date Deposited: 17 Apr 2012 13:13
Last Modified: 30 Nov 2012 17:12
URI: http://srodev.sussex.ac.uk/id/eprint/38576
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