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The hydrophobic segment of Arabidopsis thaliana cluster I diacylglycerol kinases is sufficient to target the proteins to cell membranes
Author(s) -
Vaultier Marie-Noëlle,
Cantrel Catherine,
Guerbette Françoise,
Boutté Yohann,
Vergnolle Chantal,
Çiçek Dominique,
Bolte Susanne,
Zachowski Alain,
Ruelland Eric
Publication year - 2008
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2008.04.042
Subject(s) - diacylglycerol kinase , membrane , phosphatidic acid , arabidopsis thaliana , endoplasmic reticulum , arabidopsis , chemistry , kinase , biochemistry , cytosol , microbiology and biotechnology , biology , protein kinase c , phospholipid , gene , mutant , enzyme
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 ε 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.