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The hydrophobic segment of Arabidopsis thaliana cluster I diacylglycerol kinases is sufficient to target the proteins to cell membranes
Authors:Vaultier Marie-Noëlle  Cantrel Catherine  Guerbette Françoise  Boutté Yohann  Vergnolle Chantal  Ciçek Dominique  Bolte Susanne  Zachowski Alain  Ruelland Eric
Institution:UPMC Univ Paris 06, UMR 7180, Physiologie Cellulaire et Moléculaire des Plantes, F-94200 Ivry-sur-Seine, France.
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.
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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