期刊
JOURNAL OF CELL BIOLOGY
卷 153, 期 1, 页码 207-219出版社
ROCKEFELLER UNIV PRESS
DOI: 10.1083/jcb.153.1.207
关键词
diacylglycerol kinase; lymphocytes; T cell activation; signal transduction; green fluorescent protein
类别
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 DGK alpha, an isoform highly expressed in T lymphocytes. translocates from cy tosol 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. DGK alpha -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 NH2-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 DGK alpha exerts on diacylglycerol-derived cell responses. This study is the first to describe DGK alpha as an integral component of the signaling cascades that link plasma membrane receptors to nuclear responses.
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