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• W2139547383 abstract "Diacylglycerol kinase (DGK) is suggested to attenuate diacylglycerol-induced cell responses through the phosphorylation of this second messenger to phosphatidic acid. Here, we show that DGKalpha, an isoform highly expressed in T lymphocytes, translocates from cytosol to the plasma membrane in response to two different receptors known to elicit T cell activation responses: an ectopically expressed muscarinic type I receptor and the endogenous T cell receptor. Translocation in response to receptor stimulation is rapid, transient, and requires calcium and tyrosine kinase activation. DGKalpha-mediated phosphatidic acid generation allows dissociation of the enzyme from the plasma membrane and return to the cytosol, as demonstrated using a pharmacological inhibitor and a catalytically inactive version of the enzyme. The NH(2)-terminal domain of the protein is shown to be responsible for receptor-induced translocation and phosphatidic acid-mediated membrane dissociation. After examining induction of the T cell activation marker CD69 in cells expressing a constitutively active form of the enzyme, we present evidence of the negative regulation that DGKalpha exerts on diacylglycerol-derived cell responses. This study is the first to describe DGKalpha as an integral component of the signaling cascades that link plasma membrane receptors to nuclear responses." @default.
• W2139547383 created "2016-06-24" @default.
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• W2139547383 date "2001-04-02" @default.
• W2139547383 modified "2023-10-14" @default.
• W2139547383 title "Role of Diacylglycerol Kinase α in the Attenuation of Receptor Signaling" @default.
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• W2139547383 doi "https://doi.org/10.1083/jcb.153.1.207" @default.
• W2139547383 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2185527" @default.
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