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• W1732929105 endingPage "5449" @default.
• W1732929105 startingPage "5441" @default.
• W1732929105 abstract "Abstract 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." @default.
• W1732929105 created "2016-06-24" @default.
• W1732929105 creator A5015485877 @default.
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• W1732929105 date "2004-05-01" @default.
• W1732929105 modified "2023-09-27" @default.
• W1732929105 title "A Proline-Rich Motif in the C Terminus of Akt Contributes to Its Localization in the Immunological Synapse" @default.
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• W1732929105 doi "https://doi.org/10.4049/jimmunol.172.9.5441" @default.
• W1732929105 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/15100285" @default.
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