Diacylglycerol kinase β induces filopodium formation via its C1, catalytic and carboxy-terminal domains and interacts with the Rac1-GTPase-activating protein, β2-chimaerin

Yuki Maeda, Kosuke Shibata, Rino Akiyama, Yuki Murakami, Saki Takao, Chiaki Murakami, Daisuke Takahashi, Hiromichi Sakai, Fumio Sakane

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2 Citations (Scopus)

Abstract

The β-isoform of diacylglycerol kinase (DGK) localizes predominantly to neurons and induces neurite outgrowth and spine formation. However, the detailed molecular mechanisms underlying the functions of DGKβ remain elusive. During the course of studies on other DGK isozymes, we unexpectedly found that the overexpression of wild-type DGKβ in COS-7 cells markedly induced filopodium formation. Because filopodium formation is closely related to neurite outgrowth and spine formation, we constructed various DGKβ mutants and compared their abilities to induce filopodium formation in order to elucidate the structure-function relationships of DGKβ. We found that the C-terminal, C1 and catalytic domains and catalytic activity were indispensable for filopodium formation, but the recoverin homology domain and EF-hand motifs were not. Moreover, the extent of plasma membrane localization and F-actin colocalization were positively correlated with filopodium formation. Intriguingly, DGKβ selectively interacted and colocalized at the plasma membrane with a Rac1-GTPase-activating protein, β2-chimaerin, which is an inducer of filopodia; it also interacted, to lesser extent, with α2-chimaerin, but not with α1- or β1-chimaerin. Moreover, DGKβ enhanced the plasma membrane localization of β2-chimaerin. These results suggest that DGKβ plays an important role in neurite outgrowth and spine formation in neurons via its ability to induce filopodium formation.

Original languageEnglish
Pages (from-to)54-60
Number of pages7
JournalBiochemical and Biophysical Research Communications
Volume504
Issue number1
DOIs
Publication statusPublished - Sep 26 2018

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