| First Author | Spitaler M | Year | 2006 |
| Journal | Immunity | Volume | 24 |
| Issue | 5 | Pages | 535-46 |
| PubMed ID | 16713972 | Mgi Jnum | J:113358 |
| Mgi Id | MGI:3665512 | Doi | 10.1016/j.immuni.2006.02.013 |
| Citation | Spitaler M, et al. (2006) Diacylglycerol and protein kinase D localization during T lymphocyte activation. Immunity 24(5):535-46 |
| abstractText | 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. |
