| First Author | DeFord-Watts LM | Year | 2007 |
| Journal | J Biol Chem | Volume | 282 |
| Issue | 22 | Pages | 16126-34 |
| PubMed ID | 17420248 | Mgi Jnum | J:122663 |
| Mgi Id | MGI:3715043 | Doi | 10.1074/jbc.M609418200 |
| Citation | DeFord-Watts LM, et al. (2007) The membrane-proximal portion of CD3 epsilon associates with the serine/threonine kinase GRK2. J Biol Chem 282(22):16126-34 |
| abstractText | The activation of protein kinases is one of the primary mechanisms whereby T cell receptors (TCR) propagate intracellular signals. To date, the majority of kinases known to be involved in the early stages of TCR signaling are protein-tyrosine kinases such as Lck, Fyn, and ZAP-70. Here we report a constitutive association between the TCR and a serine/threonine kinase, which was mediated through the membrane-proximal portion of CD3 epsilon. Mass spectrometry analysis of CD3 epsilon-associated proteins identified G protein-coupled receptor kinase 2 (GRK2) as a candidate Ser/Thr kinase. Transient transfection assays and Western blot analysis verified the ability of GRK2 to interact with the cytoplasmic domain of CD3 epsilon within a cell. These findings are consistent with recent reports demonstrating the ability of certain G protein-coupled receptors (GPCR) and G proteins to physically associate with the alpha/beta TCR. Because GRK2 is primarily involved in arresting GPCR signals, its interaction with CD3 epsilon may provide a novel means whereby the TCR can negatively regulate signals generated through GPCRs. |
