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Diacylglycerol kinase β promotes dendritic outgrowth and spine maturation in developing hippocampal neurons

Yasukazu Hozumi1*, Masahiko Watanabe2, Koichi Otani3 and Kaoru Goto1

Author Affiliations

1 Department of Anatomy and Cell Biology, Yamagata University School of Medicine, Yamagata 990-9585, Japan

2 Department of Anatomy, Hokkaido University School of Medicine, Sapporo 060-8638, Japan

3 Department of Psychiatry, Yamagata University School of Medicine, Yamagata 990-9585, Japan

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BMC Neuroscience 2009, 10:99  doi:10.1186/1471-2202-10-99

Published: 19 August 2009



Diacylglycerol kinase (DGK) is an enzyme that phosphorylates diacylglycerol to phosphatidic acid and comprises multiple isozymes of distinct properties. Of DGKs, mRNA signal for DGKβ is strongly detected in the striatum, and one of the transcripts derived from the human DGKβ locus is annotated in GenBank as being differentially expressed in bipolar disorder patients. Recently, we have reported that DGKβ is expressed in medium spiny neurons of the striatum and is highly concentrated at the perisynapse of dendritic spines. However, it remains elusive how DGKβ is implicated in pathophysiological role in neurons at the cellular level.


In the present study, we investigated the expression and subcellular localization of DGKβ in the hippocampus, together with its functional implication using transfected hippocampal neurons. DGKβ is expressed not only in projection neurons but also in interneurons and is concentrated at perisynaptic sites of asymmetrical synapses. Overexpression of wild-type DGKβ promotes dendrite outgrowth at 7 d in vitro (DIV) and spine maturation at 14 DIV in transfected hippocampal neurons, although its kinase-dead mutant has no effect.


In the hippocampus, DGKβ is expressed in both projection neurons and interneurons and is accumulated at the perisynapse of dendritic spines in asymmetrical synapses. Transfection experiments suggest that DGKβ may be involved in the molecular machineries of dendrite outgrowth and spinogenesis through its kinase activity.