Abstract
Recent observations suggest that diacylglycerol kinase (DGK) is one of the key enzymes involved in the regulation of signal transduction. It attenuates protein kinase C activity and cell cycle progression of T-lymphocytes, through controlling the intracellular levels of the second messengers, diacylglycerol and phosphatidic acid. To date, eight DGK isozymes containing characteristic zinc finger structures in common have been identified. Type I DGKs (α, β and γ) contain EF-hand motifs that contribute to the calcium-dependent activities of this type of DGK. A pleckstrin homology and/or an EPH C-terminal tail homology domains are found in type II isozymes (DGKδ and η). DGKϵ represents a third type of DGK that selectively phosphorylates arachidonate-containing diacylglycerol. DGKζ (type IV) and DGKθ (type V) contain four tandem ankyrin repeats and a Ras-associating domain, respectively.
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