| First Author | Kane LP | Year | 2004 |
| Journal | J Immunol | Volume | 172 |
| Issue | 9 | Pages | 5441-9 |
| PubMed ID | 15100285 | Mgi Jnum | J:89654 |
| Mgi Id | MGI:3041020 | Doi | 10.4049/jimmunol.172.9.5441 |
| Citation | Kane LP, et al. (2004) A proline-rich motif in the C terminus of Akt contributes to its localization in the immunological synapse. J Immunol 172(9):5441-9 |
| abstractText | The serine/threonine kinases of the Akt/protein kinase B family are regulated in part by recruitment to the plasma membrane, which is accomplished by the binding of an N-terminal PH domain to the phosphatidylinositol 3-kinase products phosphoinositol 3,4,5-trisphosphate and phosphoinositol 3,4-bisphosphate. We have examined Akt localization in a murine T cell clone (D10) before and after stimulation by APC/Ag, and we found that whereas the pleckstrin homology domain is required for plasma membrane recruitment of Akt upon T cell activation, the C terminus of the kinase restricts its cellular localization to the immunologic synapse formed at the site of T cell/APC contact. A recently described proline-rich motif in this region appears to be important for proper localization of full-length Akt. Moreover, a form of Akt in which this motif was mutated acts as a potent dominant negative construct to block T cell activation. Therefore, multiple mechanisms are involved in the proper targeting of Akt during the early events of T cell activation. |
