The hydrophobic segment of Arabidopsis thaliana cluster I diacylglycerol kinases is sufficient to target the proteins to cell membranes |
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Authors: | Vaultier Marie-Noëlle Cantrel Catherine Guerbette Françoise Boutté Yohann Vergnolle Chantal Ciçek Dominique Bolte Susanne Zachowski Alain Ruelland Eric |
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Affiliation: | UPMC Univ Paris 06, UMR 7180, Physiologie Cellulaire et Moléculaire des Plantes, F-94200 Ivry-sur-Seine, France. |
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Abstract: | Diacylglycerol kinases (DGKs) catalyze the phosphorylation of diacylglycerol into phosphatidic acid. To fulfill their role in many signalling processes, DGKs must be located at, or in, membranes. Most mammalian DGKs are cytosolic and are recruited to membranes upon stimulation, except for epsilon type DGKs that are permanently membrane-associated through a hydrophobic segment. Nothing is known about the mechanism(s) involved in the membrane localization of plant DGKs. By fusion to fluorescent proteins, we show that two DGKs from cluster I in Arabidopsis thaliana possess amino-terminal hydrophobic segments that are sufficient to address them to endoplasmic reticulum membranes. |
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Keywords: | ATPase, adenosine triphosphatase DAG, diacylglycerol DGK, diacylglycerol kinase G-6-Pase, glucose-6-phosphatase ER, endoplasmic reticulum GFP, green fluorescent protein PA, phosphatidic acid PI, phosphatidylinositol PLC, phospholipase C UDPase, uridine diphosphatase YFP, yellow fluorescent protein |
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