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AKT1/PKBα is recruited to lipid rafts and activated downstream of PKC isotypes in CD3‐induced T cell signaling
Author(s) -
Bauer Birgit,
Jenny Marcel,
Fresser Fiedrich,
Überall Florian,
Baier Gottfried
Publication year - 2003
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(03)00287-4
Subject(s) - lipid raft , microbiology and biotechnology , protein kinase b , akt1 , downstream (manufacturing) , phosphorylation , protein kinase c , signal transduction , chemistry , biology , operations management , economics
Protein kinase (PK) Cθ and Akt/PKBα cooperate in T cell receptor/CD28‐induced T cell signaling. We here demonstrate the recruitment of endogenous Akt1 and PKCθ to lipid rafts in CD3‐stimulated T cells. Further we show that Myr‐PKCθ mediates translocation of endogenous Akt1 to the plasma membrane as well as to lipid rafts, most likely explained by the observed complex formation of both protein kinases. In addition, in peripheral mouse T cells, the PKC inhibitor Gö6850 could partially block Akt1 activation in CD3‐induced signaling, placing PKC isotype(s) upstream of Akt1. However, T cells derived from PKCθ knockout mice were not impaired in CD3‐ or phorbol ester‐induced Akt1 activity. Taken together, the results of this study give new insights into the functional link of Akt1 and PKCθ in T cell signaling, demonstrating the co‐recruitment of the two kinases and showing a novel pathway leading to Akt1 transactivation where PKC isotype(s) are involved but PKCθ is not essential.