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Vol. 13, Issue 1, 302-316, January 2002

Diacylglycerol Kinase  Suppresses ER-to-Golgi Traffic via Its SAM and PH Domains

Hisao Nagaya,^* Ikuo Wada,^* Yan-Jun Jia,^* and Hideo Kanoh^*

 ^*Department of Biochemistry, Sapporo Medical University School of Medicine, Sapporo 060-8556, Japan;  Core Research for Evolutional Science and Technology, JST, Japan

We report here that the anterograde transport from the endoplasmic reticulum (ER) to the Golgi was markedly suppressed by diacylglycerol kinase  (DGK) that uniquely possesses a pleckstrin homology (PH) and a sterile  motif (SAM) domain. A low-level expression of DGK in NIH3T3 cells caused redistribution into the ER of the marker proteins of the Golgi membranes and the vesicular-tubular clusters (VTCs). In this case DGK delayed the ER-to-Golgi traffic of vesicular stomatitis virus glycoprotein (VSV G) and also the reassembly of the Golgi apparatus after brefeldin A (BFA) treatment and washout. DGK was demonstrated to associate with the ER through its C-terminal SAM domain acting as an ER-targeting motif. Both of the SAM domain and the N-terminal PH domain of DGK were needed to exert its effects on ER-to-Golgi traffic. Kinase-dead mutants of DGK were also effective as the wild-type enzyme, suggesting that the catalytic activity of DGK was not involved in the present observation. Remarkably, the expression of DGK abrogated formation of COPII-coated structures labeled with Sec13p without affecting COPI structures. These findings indicate that DGK negatively regulates ER-to-Golgi traffic by selectively inhibiting the formation of ER export sites without significantly affecting retrograde transport.

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Corresponding author. E-mail address: wada{at}sapmed.ac.jp.

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Molecular Biology of the Cell
Vol. 13, 302-316, January 2002
Copyright © 2002 by The American Society for Cell Biology

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