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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
Full text not available from this repository.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://sro.sussex.ac.uk/id/eprint/38576 |